wanglab/gogpt-training-data huggingface dataset:
Protein: Methyl-branched lipid omega-hydroxylase (EC 1.14.15.14) (Cholest-4-en-3-one C26-monooxygenase) (Cholest-4-en-3-one C26-monooxygenase [(25R)-3-oxocholest-4-en-26-oate forming]) (Cholesterol C26-monooxygenase) (Cholesterol C26-monooxygenase [(25R)-3beta-hydroxycholest-5-en-26-oate forming]) (Cytochrome P450 124) (Steroid C26-monooxygenase) (EC 1.14.15.28) (Steroid C27-monooxygenase) (P9WPP3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Primarily hydroxylates the omega-carbon of a number of methyl-branched lipids, including (2E,6E)-farnesol, phytanate, geranylgeraniol, 15-methylpalmitate and (2E,6E)-farnesyl diphosphate. Also catalyzes the sequential oxidation of the terminal methyl of cholest-4-en-3-one into (25R)-26-hydroxycholest-4-en-3-one (alcohol), (25R)-26-oxocholest-4-en-3-one (aldehyde), to finally yield the carboxylic acid (25R)-3-oxocholest-4-en-26-oate. Cyp124 catalyzes preferentially the oxidation of (25R)-26-hydroxycholest-4-en-3-one diastereomer. Also able to sequentially oxidize cholesterol itself, not only cholest-4-en-3-one.
Interaction partners:
- Polyketide synthase Pks13
- Putative cytochrome P450 138
- Possible oxygenase
- Peptide synthetase MbtE
- Putative cytochrome P450 139
- Probable oxidoreductase
- 3-ketosteroid-9-alpha-monooxygenase, ferredoxin reductase component
- Putative cytochrome P450 132
- Omega-hydroxy-beta-dihydromenaquinone-9 sulfotransferase Stf3
- Putative inactive phenolphthiocerol synthesis polyketide synthase type I Pks1
Sequence:
MGLNTAIATRVNGTPPPEVPIADIELGSLDFWALDDDVRDGAFATLRREAPISFWPTIELPGFVAGNGHWALTKYDDVFYASRHPDIFSSYPNITINDQTPELAEYFGSMIVLDDPRHQRLRSIVSRAFTPKVVARIEAAVRDRAHRLVSSMIANNPDRQADLVSELAGPLPLQIICDMMGIPKADHQRIFHWTNVILGFGDPDLATDFDEFMQVSADIGAYATALAEDRRVNHHDDLTSSLVEAEVDGERLSSREIASFFILLVVAGNETTRNAITHGVLALSRYPEQRDRWWSDFDGLAPTAVEEIVRWASPVVYMRRTLTQDIELRGTKMAAGDKVSLWYCSANRDESKFADPWTFDLARNPNPHLGFGGGGAHFCLGANLARREIRVAFDELRRQMPDVVATEEPARLLSQFIHGIKTLPVTWS
Protein: Stimulator of interferon genes protein (NvSTING) (STING) (A7SLZ2)
Organism: Nematostella vectensis (Starlet sea anemone)
Function: Sensor of cytosolic DNA from bacteria and viruses that promotes autophagy. Acts by recognizing and binding cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA in the cytosol. Following cGAMP-binding, promotes the formation of autophagosomes, leading to target cytosolic DNA for degradation by the lysosome. Exhibits guanine base-specific ligand recognition. Binds 3'-3'linked cGAMP, 2'-3' linked cGAMP and 3'-3' linked c-di-GMP with much greater affinity as compared to 3'-3' linked c-di-AMP. Lacks the C-terminal tail (CTT) found in mammalian orthologs which is essential for interferon signaling.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein kinase domain-containing protein
Sequence:
MRRAEENNGFGTIPKRRNQHTPFYASIGMIVVIIVAFTSYHITSYGDDRNRAMRQYSFTFSLAYLAFLVGELLRRCCLFAEEYRHIETRYNGSLKKAIQTTFSFGHNNVLFVASLLFFVVFVASNDPNGSSSVIQGNSTAEPHTEMRQTSGWQGLWGQFIISALLTPLVVHLLGLRELSKVEESQLNEKENKNVADGLAWSYYFGYLKFVLPELEKQIEKTSKFRSKEKFVKKMFILIPSNCFWDDKIPGSDYDPQNRITFEGNTEPLEKTRGGVFLRHYKHSVYEIKDGENEPWFCIMEYATPLLTLYDMSVAQPGELSREERDAQVVVFLRKLQDILEGDRACQGKYELVTFSPDRDLADVMLRKLKDSELEIGG
Protein: Cytoplasmic dynein 2 intermediate chain 2 (Dynein 2 intermediate chain 2) (WD repeat-containing protein 34) (Q96EX3)
Organism: Homo sapiens (Human)
Function: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 2 complex (dynein-2 complex), a motor protein complex that drives the movement of cargos along microtubules within cilia and flagella in concert with the intraflagellar transport (IFT) system. DYNC2I2 plays a major role in retrograde ciliary protein trafficking and in ciliogenesis. Required also to maintain a functional transition zone.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19521662, ECO:0000269|PubMed:25205765}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:19521662, ECO:0000269|PubMed:25205765}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:19521662}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:25205765}. Cell projection, cilium {ECO:0000269|PubMed:25205765}. Cell projection, filopodium {ECO:0000250|UniProtKB:Q5U4F6}. Note=Concentrates around the centrioles and basal bodies also showing axonemal staining. {ECO:0000250|UniProtKB:Q5U4F6}.
Interaction partners:
- Cytoplasmic dynein 2 heavy chain 1
- Cytoplasmic dynein 2 intermediate chain 1
- Cytoplasmic dynein 2 light intermediate chain 1
- Dynein light chain 1, cytoplasmic
- Dynein light chain roadblock-type 1
- Dynein light chain Tctex-type protein 2B
- Dynein light chain Tctex-type 3
- Dynein light chain Tctex-type 1
- Dynein light chain roadblock-type 2
- Dynein light chain 2, cytoplasmic
Sequence:
MATRAQPGPLSQAGSAGVAALATVGVASGPGPGRPGPLQDETLGVASVPSQWRAVQGIRWETKSCQTASIATASASAQARNHVDAQVQTEAPVPVSVQPPSQYDIPRLAAFLRRVEAMVIRELNKNWQSHAFDGFEVNWTEQQQMVSCLYTLGYPPAQAQGLHVTSISWNSTGSVVACAYGRLDHGDWSTLKSFVCAWNLDRRDLRPQQPSAVVEVPSAVLCLAFHPTQPSHVAGGLYSGEVLVWDLSRLEDPLLWRTGLTDDTHTDPVSQVVWLPEPGHSHRFQVLSVATDGKVLLWQGIGVGQLQLTEGFALVMQQLPRSTKLKKHPRGETEVGATAVAFSSFDPRLFILGTEGGFPLKCSLAAGEAALTRMPSSVPLRAPAQFTFSPHGGPIYSVSCSPFHRNLFLSAGTDGHVHLYSMLQAPPLTSLQLSLKYLFAVRWSPVRPLVFAAASGKGDVQLFDLQKSSQKPTVLIKQTQDESPVYCLEFNSQQTQLLAAGDAQGTVKVWQLSTEFTEQGPREAEDLDCLAAEVAA
Protein: Natural cytotoxicity triggering receptor 3 ligand 1 (B7 homolog 6) (B7-H6) (Q68D85)
Organism: Homo sapiens (Human)
Function: Triggers NCR3-dependent natural killer cell activation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19528259}; Single-pass type I membrane protein {ECO:0000269|PubMed:19528259}.
Interaction partners:
- Natural cytotoxicity triggering receptor 3
- Natural cytotoxicity triggering receptor 2
- Natural cytotoxicity triggering receptor 1
- Prostaglandin D2 receptor 2
- CD276 antigen
- CD226 antigen
- Programmed cell death 1 ligand 1
- Nectin-2
- Natural killer cells antigen CD94
- Poliovirus receptor
Sequence:
MTWRAAASTCAALLILLWALTTEGDLKVEMMAGGTQITPLNDNVTIFCNIFYSQPLNITSMGITWFWKSLTFDKEVKVFEFFGDHQEAFRPGAIVSPWRLKSGDASLRLPGIQLEEAGEYRCEVVVTPLKAQGTVQLEVVASPASRLLLDQVGMKENEDKYMCESSGFYPEAINITWEKQTQKFPHPIEISEDVITGPTIKNMDGTFNVTSCLKLNSSQEDPGTVYQCVVRHASLHTPLRSNFTLTAARHSLSETEKTDNFSIHWWPISFIGVGLVLLIVLIPWKKICNKSSSAYTPLKCILKHWNSFDTQTLKKEHLIFFCTRAWPSYQLQDGEAWPPEGSVNINTIQQLDVFCRQEGKWSEVPYVQAFFALRDNPDLCQCCRIDPALLTVTSGKSIDDNSTKSEKQTPREHSDAVPDAPILPVSPIWEPPPATTSTTPVLSSQPPTLLLPLQ
Protein: Trypanosoma vivax (Q57VD0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPLQPSYLMRPPKACSVYPTCVFIFWEAPRAVTQVDEVENITGQLRPSLVQWSYVVEWTTNNSPKTEVAEMFTASSHAVLELLYPQETLQVRIVARGSCDGSEITRVSTSCTVEPGLAVALPWLHPRSMRCLCIFDALFFSYSGIHCVDAIPSSWKHVRAKMESVRLLESRFSCAIVKAVYEEPPYPITSTTVYYFVMCPKALVNPRDKLRHCDIKYLLERDQEQKPCAVFCGIGETGSSAALAAHLFISAIPPSSNELCSRVFCIAYGSPRRLLVEDYLVLASSPPFAGNFLHYTALLAPKDPLFEFTGDVLNSDAPVGVSGAAAGGGSPKEVHAVQHFNMPLGVRCGPVFDGTSGNVHLEARCSGVETLGREECNELLDVSTHLSMLNQLILQCYHSGDTGDILVPMINNVQHAMEDGVTVFLTIEGESLHFGPRVICTSSRNQAMAAVSVTAVTPTRLTATFSLMDMLTTKFFARHRRPPQSLLVEISLFTDHGYVSFNEYRIVIAEDISLLLFHSSHSDGPHQWIFGPPGDLVDGAISVEPLLTSLVAGGPNTSTFVPFQSTSLLSDIAAVSELVGKHAVKKPETGLYNFIFRGAAQSTKPISIGSIPMHEAVLLKDALKRHAASETRDPNALRSELDPWKRRLLARLPSLDSGNYREKLLSLLLMLGGPKPAADTTAVALETLLLSKVLHNLRRSQNAIHLNYTNSLSTCMGFDVFYERMLPLALAWVKHSEEAELEALHNIATLWIACLLYHLRGAYLFTHAVVVAGCAGSGCNTLCHAIVRERAARQHHFVGTQRERVIVVRRAKLGSLADVKEALARGLGITAIVCGELSDVAGKEFFDLWCSLRRMLCRRMAQRLFAFLSKVDELLGRNQLIKPLEEACIGAEGGAVAFQSLQRQAALAARTEWDVGSEKRGEDASLAGFVAVSFAPSVLLLRNSPFVHSSGMSAEEFAQKLMSISSYQLRRVLAGIVEGEFVNAR
Protein: Collagen alpha-2(VI) chain (P12110)
Organism: Homo sapiens (Human)
Function: Collagen VI acts as a cell-binding protein.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:8305732}. Membrane {ECO:0000269|PubMed:8305732}; Peripheral membrane protein {ECO:0000269|PubMed:8305732}. Note=Recruited on membranes by CSPG4.
Interaction partners:
- Collagen alpha-1
- Collagen alpha-3
- Collagen alpha-1
- CD44 antigen
- Platelet glycoprotein VI
- Collagen alpha-2
- Collagen alpha-1
- Integrin alpha-5
- Integrin alpha-1
- Integrin alpha-11
Sequence:
MLQGTCSVLLLWGILGAIQAQQQEVISPDTTERNNNCPEKTDCPIHVYFVLDTSESVTMQSPTDILLFHMKQFVPQFISQLQNEFYLDQVALSWRYGGLHFSDQVEVFSPPGSDRASFIKNLQGISSFRRGTFTDCALANMTEQIRQDRSKGTVHFAVVITDGHVTGSPCGGIKLQAERAREEGIRLFAVAPNQNLKEQGLRDIASTPHELYRNDYATMLPDSTEIDQDTINRIIKVMKHEAYGECYKVSCLEIPGPSGPKGYRGQKGAKGNMGEPGEPGQKGRQGDPGIEGPIGFPGPKGVPGFKGEKGEFGADGRKGAPGLAGKNGTDGQKGKLGRIGPPGCKGDPGNRGPDGYPGEAGSPGERGDQGGKGDPGRPGRRGPPGEIGAKGSKGYQGNSGAPGSPGVKGAKGGPGPRGPKGEPGRRGDPGTKGSPGSDGPKGEKGDPGPEGPRGLAGEVGNKGAKGDRGLPGPRGPQGALGEPGKQGSRGDPGDAGPRGDSGQPGPKGDPGRPGFSYPGPRGAPGEKGEPGPRGPEGGRGDFGLKGEPGRKGEKGEPADPGPPGEPGPRGPRGVPGPEGEPGPPGDPGLTECDVMTYVRETCGCCDCEKRCGALDVVFVIDSSESIGYTNFTLEKNFVINVVNRLGAIAKDPKSETGTRVGVVQYSHEGTFEAIQLDDERIDSLSSFKEAVKNLEWIAGGTWTPSALKFAYDRLIKESRRQKTRVFAVVITDGRHDPRDDDLNLRALCDRDVTVTAIGIGDMFHEKHESENLYSIACDKPQQVRNMTLFSDLVAEKFIDDMEDVLCPDPQIVCPDLPCQTELSVAQCTQRPVDIVFLLDGSERLGEQNFHKARRFVEQVARRLTLARRDDDPLNARVALLQFGGPGEQQVAFPLSHNLTAIHEALETTQYLNSFSHVGAGVVHAINAIVRSPRGGARRHAELSFVFLTDGVTGNDSLHESAHSMRKQNVVPTVLALGSDVDMDVLTTLSLGDRAAVFHEKDYDSLAQPGFFDRFIRWIC
Protein: Large ribosomal subunit protein uL3 (60S ribosomal protein L3) (L4) (P21531)
Organism: Rattus norvegicus (Rat)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:P39023}. Cytoplasm {ECO:0000250|UniProtKB:P39023}.
Interaction partners:
- Large ribosomal subunit protein eL18
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein uL4
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein uL13
- Small ribosomal subunit protein eS1
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein eS1
- Large ribosomal subunit protein uL18
Sequence:
MSHRKFSAPRHGSLGFLPRKRSSRHRGKVKSFPKDDPSKPVHLTAFLGYKAGMTHIVREVDRPGSKVNKKEVVEAVTIVETPPMVVVGIVGYVETPRGLRTFKTVFAEHISDECKRRFYKNWHKSKKKAFTKYCKKWQDDTGKKQLEKDFNSMKKYCQVIRIIAHTQMRLLPLRQKKAHLMEIQVNGGTVAEKLDWARERLEQQVPVNQVFGQDEMIDVIGVTKGKGYKGVTSRWHTKKLPRKTHRGLRKVACIGAWHPARVAFSVARAGQKGYHHRTEINKKIYKIGQGYLIKDGKLIKNNASTDYDLSDKSINPLGGFVHYGEVTNDFIMLKGCVVGTKKRVLTLRKSLLVQTKRRALEKIDLKFIDTTSKFGHGRFQTMEEKKAFMGPLKKDRIAKEEGA
Protein: Serine/threonine-protein kinase A-Raf (EC 2.7.11.1) (Proto-oncogene A-Raf) (Proto-oncogene A-Raf-1) (P14056)
Organism: Rattus norvegicus (Rat)
Function: Involved in the transduction of mitogenic signals from the cell membrane to the nucleus. May also regulate the TOR signaling cascade (By similarity).
Interaction partners:
- GTPase NRas
- 14-3-3 protein zeta/delta
- Dual specificity mitogen-activated protein kinase kinase 1
- GTPase HRas
- Ras-related protein Rap-1A
- Dual specificity mitogen-activated protein kinase kinase 2
- 14-3-3 protein beta/alpha
- Ras-related protein Rap-1b
- 14-3-3 protein gamma
- 14-3-3 protein theta
Sequence:
MEPPRGPPASGAEPSRAVGTVKVYLPNKQRTVVTVRDGMSVYDSLDKALKVRGLNQDCCVVYRLIKGRKTVTAWDTAIAPLDGEELIVEVLEDVPLTMHNFVRKTFFSLAFCDFCLKFLFHGFRCQTCGYKFHQHCSSKVPTVCVDMSTNRRQFYHSIQDLSGGSRQQEVPSNLSVNELLTPQGPSPFTQQRDQEHFSFPAPANPPLQRIRSTSTPNVHMVSTTAPMDSSLMQFTAQSFSTDAAGRGGDGAPRGSPSPASVSSGRKSPHSKLPAEQRERKSLADEKKKVKNLGYRDSGYYWEVPPSEVQLLKRIGTGSFGTVFRGRWHGDVAVKVLKVAQPTAEQAQAFKNEMQVLRKTRHVNILLFMGFMTRPGFAIITQWCEGSSLYHHLHVADTRFDMVQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLATVKTRWSGAQPLEQPSGSVLWMAAEVIRMQDPNPYSFQSDVYAYGVVLYELMTGSLPYSHIGSRDQIIFMVGRGYLSPDLSKIFSNCPKAMRRLLTDCLKFQREERPLFPQILATIELLQRSLPKIERSASEPSLHRTQADELPACLLSAARLVP
Protein: Cytokine-inducible SH2-containing protein (CIS) (CIS-1) (Suppressor of cytokine signaling) (SOCS) (Q62225)
Organism: Mus musculus (Mouse)
Function: SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. CIS is involved in the negative regulation of cytokines that signal through the JAK-STAT5 pathway such as erythropoietin, prolactin and interleukin 3 (IL3) receptor. Inhibits STAT5 trans-activation by suppressing its tyrosine phosphorylation. May be a substrate-recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity).
Interaction partners:
- Cullin-5
- Elongin-B
- Signal transducer and activator of transcription 3
- Signal transducer and activator of transcription
- RING-box protein 2
- Signal transducer and activator of transcription 1
- Elongin-C
- Signal transducer and transcription activator 6
- Signal transducer and activator of transcription 2
- Signal transducer and activator of transcription 5B
Sequence:
MVLCVQGSCPLLAVEQIGRRPLWAQSLELPGPAMQPLPTGAFPEEVTEETPVQAENEPKVLDPEGDLLCIAKTFSYLRESGWYWGSITASEARQHLQKMPEGTFLVRDSTHPSYLFTLSVKTTRGPTNVRIEYADSSFRLDSNCLSRPRILAFPDVVSLVQHYVASCAADTRSDSPDPAPTPALPMSKQDAPSDSVLPIPVATAVHLKLVQPFVRRSSARSLQHLCRLVINRLVADVDCLPLPRRMADYLRQYPFQL
Protein: Steroid 5-alpha-reductase DET2 (LeDET2) (EC 1.3.1.22) (Q5K2N1)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Function: Involved in a reduction step in the biosynthesis of the plant steroid, brassinolide (BL). Can use progesterone, testosterone, androstenedione and campestenone as substrate.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cytochrome P450 90B1
- 22alpha-hydroxysteroid 23-monooxygenase
- 22alpha-hydroxysteroid 23-monooxygenase
- CYP90A1-like protein
- Cytochrome P450 724B1
- Steroid 5-alpha reductase C-terminal domain-containing protein
- Cytochrome P450 85A1
- Cytochrome P450 85A3
Sequence:
MFSSDENLFNFIVFFILVMAFPTFILCQFFTSPYGKHYTSADSGTTISPPIAWAFMESPTLWLTIIVFRLGKNYTNPLAFLLISPYLFHYTNRTIIYPLRLRSRNTKNNFPLNIAVTAFIFNLLNAYIQSRWVSHYANYQEDDWFWVRFGIGLVIFGSGMLLNIWADGVLLGLKSQGGGYKIPRGGLFDYVSSPNYLGEIMEWLGWALMTWSWAGLAFFVYTCANLVPRAVSNHKWYLQKFGEDYPKNRKAVFPFLY
Protein: Histone-lysine N-methyltransferase (EC 2.1.1.355) (A0A8I6AJD7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Chromosome, centromere {ECO:0000256|ARBA:ARBA00004584}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR009343}.
Interaction partners:
Sequence:
ALIKALTSGCSVCCKSSWNQLQDLCRLAKLSCPALGVSKKNLYDFEVEYLCDYKKIREQEYYLVKWRGYPDSENTWEPRQNLKCVRILKQFHKDLERELVRRHRRSKPPRHLDPNLANYLVQKAKQRRALQRWEQELNAKRSHLGRITVENEVDLDGPPRSFVYINEYRVGEGITLNQVAVGCECQDCLLAPTGGCCPGASLHKFAYNDQGQVRLKAGQPIYECNSRCCCGYDCPNRVVQKGIRYNLCIFRTDDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDYVEDVYTVDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIWAGEELTFDYNMQVDPVDMESTRMDSNFGLAGLPGSPKKRVRIECKCGTTACRKYLF
Protein: Alpha-globin transcription factor CP2 (SAA3 enhancer factor) (Transcription factor LSF) (Q12800)
Organism: Homo sapiens (Human)
Function: Binds a variety of cellular and viral promoters including fibrinogen, alpha-globin, SV40 and HIV-1 promoters. Activation of the alpha-globin promoter in erythroid cells is via synergistic interaction with UBP1 (By similarity). Functions as part of the SSP (stage selector protein) complex. Facilitates the interaction of the gamma-globin genes with enhancer elements contained in the locus control region in fetal erythroid cells. Interacts by binding to the stage selector element (SSE) in the proximal gamma-globin promoter.
Subcellular location: Nucleus {ECO:0000269|PubMed:1732747, ECO:0000269|PubMed:7828600, ECO:0000269|PubMed:8114710}.
Interaction partners:
- Amyloid beta precursor protein binding family B member 1
- Thymidylate synthase
- Upstream-binding protein 1
- Transcription factor NF-E4
- Dihydropyrimidine dehydrogenase [NADP
- Protein LYRIC
- Ankyrin repeat domain-containing protein 29
- E3 ubiquitin-protein ligase RING2
Sequence:
MAWALKLPLADEVIESGLVQDFDASLSGIGQELGAGAYSMSDVLALPIFKQEESSLPPDNENKILPFQYVLCAATSPAVKLHDETLTYLNQGQSYEIRMLDNRKLGELPEINGKLVKSIFRVVFHDRRLQYTEHQQLEGWRWNRPGDRILDIDIPMSVGIIDPRANPTQLNTVEFLWDPAKRTSVFIQVHCISTEFTMRKHGGEKGVPFRVQIDTFKENENGEYTEHLHSASCQIKVFKPKGADRKQKTDREKMEKRTPHEKEKYQPSYETTILTECSPWPEITYVNNSPSPGFNSSHSSFSLGEGNGSPNHQPEPPPPVTDNLLPTTTPQEAQQWLHRNRFSTFTRLFTNFSGADLLKLTRDDVIQICGPADGIRLFNALKGRMVRPRLTIYVCQESLQLREQQQQQQQQQQKHEDGDSNGTFFVYHAIYLEELTAVELTEKIAQLFSISPCQISQIYKQGPTGIHVLISDEMIQNFQEEACFILDTMKAETNDSYHIILK
Protein: Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase (EC 2.7.4.24) (Q54PE2)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|RuleBase:RU365032}.
Interaction partners:
- Kinase
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase
- Uncharacterized protein
- Ankyrin repeat-containing protein
- F-box domain-containing protein
- Inositol-tetrakisphosphate 1-kinase
- HECT-type E3 ubiquitin transferase
Sequence:
MAKISLGICCMEEKLKCNVMKYFIKKLKEFKELEIIEFDSNTIFNLPIQEWPIVDSFLSFYSNGFPLEKAIRYWKLRRPYLVNDLELQLLLQDRQKVNKILEDNNIPCPKSLYVLRDPITNNLITPNFNQSDDYIEVNGNRIYKPFIEKPFNSDDHNNYIYYPKSQGGGCRKLFRKVGNNSSDYFNDINTIRDKGSYTYEEFLKIDDFKDVKIYSTKSFSYSELRKSPSVDGFVERTTMGKEKRSVTNLSDQEVNISFKINKAFKQFVCGFDILRVNGISYVCDVNGWSFVKGDHFKTFYDSTSKSLFEKLFNHFKNRNTIITNINTNTIHNCSIGIAENAPQPSSTNTSPEQPTFDFSPSSSPTNLYPSSSSPLFNLNLNNLNNLNNLNNNNNSNNNSIGNDQNNSNSTVTTPPHFDLISSSAYDKHHQDIFSRHIRVYNHQNLNLNNNNNNNNKNNNNNNNNIFSTISSSISVDDSFTGSAI
Protein: Beta-ketoacyl-[acyl-carrier-protein] synthase III (Beta-ketoacyl-ACP synthase III) (KAS III) (EC 2.3.1.180) (3-oxoacyl-[acyl-carrier-protein] synthase 3) (3-oxoacyl-[acyl-carrier-protein] synthase III) (A0A140N913)
Organism: Escherichia coli (strain B / BL21-DE3)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01815}.
Interaction partners:
Sequence:
MYTKIIGTGSYLPEQVRTNADLEKMVDTSDEWIVTRTGIRERHIAAQNETVSTMGFEAATRAIEMAGIEKDQIGLIVVATTSATHAFPSAACQIQSMLGIKGCPAFDVAAACAGFTYALSVADQYVKSGAVKYALVVGSDVLARTCDPTDRGTIIIFGDGAGAAVLAASEEPGIISTHLHADGSYGELLTLPNADRVNPENSIHLTMAGNEVFKVAVTELAHIVDETLAANNLDRSQLDWLVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIKPGQLVLLEAFGGGFTWGSALVRF
Protein: SR-CI (Q5ELU2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEFFWTLAVIVIYCIGHIHGRCERSLDLDNGSINYRQRNIVRFRCNRGYTLQGTVMQTCDRDGRLRGEKPFCASRGCARPEDPENGHVENLSLRADVVCHDGYVLVGGRTAYCDGERWSTQLGSCRRSNHTRDHSCDFESEDQCGWEAETTFRRPWKRVSTVSDIHSLRTGPRHDHTFKNESGGHYMRMETQMGAYGSYHLLSPIYPRSLTLKTACCFRFHYFMFGAGVDNLVVSVKPVSMPMATMWNRFRANCSKFEISGQQGTQWLEHTISIDEMQEDFQVIFTATDARSQFGDIAIDDVKLMTGSECGTNGFSTTTEPTAPTGSNEQPLVYDMMSCSGRCGTPISTSNITNNGIVMGCGCNDECLSDETCCLNYLEECTKELLTTTEDDISSLPPTVTSTSTSTTRKSTTTTTTSTTTTSTTTTKRPTTTTTTTKATTTKRTTTTKKPTTTSTTPKPTTTTSTTPKSTTSTTFTTSTTSTRPTTTTTINVFTTKKTTIMIPTSSTEKTTGINTTMKTRKRITWNVDPQDIEGHMDTSGSTPNPALVVLYLLLAIVLVVVLANVVNRWIIPITGSKTSSEKAVRFKKAFDSLKKQRKRNSMDDQPLCDSDNDDVEYFEEMGVDIRHRTDL
Protein: Dihydrolipoyl dehydrogenase (LPD) (EC 1.8.1.4) (Component of peroxynitrite reductase/peroxidase complex) (Component of PNR/P) (Dihydrolipoamide dehydrogenase) (E3 component of alpha-ketoacid dehydrogenase complexes) (P9WHH9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Lipoamide dehydrogenase is an essential component of the alpha-ketoacid dehydrogenase complexes, namely the pyruvate dehydrogenase (PDH) complex, the branched-chain alpha-ketoacid dehydrogenase (BCKADH) complex, and likely also the 2-oxoglutarate dehydrogenase (ODH) complex. Catalyzes the reoxidation of dihydrolipoyl groups which are covalently attached to the lipoate acyltransferase components (E2) of the complexes. Is also able to catalyze the transhydrogenation of NADH and thio-NAD(+) in the absence of D,L-lipoamide, and the NADH-dependent reduction of quinones in vitro.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
- Multifunctional 2-oxoglutarate metabolism enzyme
- 3-methyl-2-oxobutanoate dehydrogenase subunit beta
- Dihydrolipoyllysine-residue acyltransferase component of branched-chain alpha-ketoacid dehydrogenase complex
- 3-methyl-2-oxobutanoate dehydrogenase subunit alpha
- Pyruvate dehydrogenase E1 component
- Glycine cleavage system H protein
- Aminomethyltransferase
- Probable glycine dehydrogenase
- 2-oxoglutarate oxidoreductase subunit KorA
Sequence:
MTHYDVVVLGAGPGGYVAAIRAAQLGLSTAIVEPKYWGGVCLNVGCIPSKALLRNAELVHIFTKDAKAFGISGEVTFDYGIAYDRSRKVAEGRVAGVHFLMKKNKITEIHGYGTFADANTLLVDLNDGGTESVTFDNAIIATGSSTRLVPGTSLSANVVTYEEQILSRELPKSIIIAGAGAIGMEFGYVLKNYGVDVTIVEFLPRALPNEDADVSKEIEKQFKKLGVTILTATKVESIADGGSQVTVTVTKDGVAQELKAEKVLQAIGFAPNVEGYGLDKAGVALTDRKAIGVDDYMRTNVGHIYAIGDVNGLLQLAHVAEAQGVVAAETIAGAETLTLGDHRMLPRATFCQPNVASFGLTEQQARNEGYDVVVAKFPFTANAKAHGVGDPSGFVKLVADAKHGELLGGHLVGHDVAELLPELTLAQRWDLTASELARNVHTHPTMSEALQECFHGLVGHMINF
Protein: Tripartite motif-containing protein 49 (RING finger protein 18) (Testis-specific RING-finger protein) (P0CI25)
Organism: Homo sapiens (Human)
Interaction partners:
- Tripartite motif-containing protein 49C
- Cyclin-dependent kinases regulatory subunit 1
- Gamma-butyrobetaine dioxygenase
Sequence:
MNSGILQVFQGELICPLCMNYFIDPVTIDCGHSFCRPCFYLNWQDIPFLVQCSECTKSTEQINLKTNIHLKKMASLARKVSLWLFLSSEEQMCGTHRETKKIFCEVDRSLLCLLCSSSQEHRYHRHRPIEWAAEEHREKLLQKMQSLWEKACENHRNLNVETTRTRCWKDYVNLRLEAIRAEYQKMPAFHHEEEKHNLEMLKKKGKEIFHRLHLSKAKMAHRMEILRGMYEELNEMCHKPDVELLQAFGDILHRSESVLLHMPQPLNPELSAGPITGLRDRLNQFRVHITLHHEEANNDIFLYEILRSMCIGCDHQDVPYFTATPRSFLAWGVQTFTSGKYYWEVHVGDSWNWAFGVCNMYRKEKNQNEKIDGKAGLFLLGCVKNDIQCSLFTTSPLMLQYIPKPTSRVGLFLDCEAKTVSFVDVNQSSLIYTIPNCSFSPPLRPIFCCIHF
Protein: tRNA (guanosine(18)-2'-O)-methyltransferase (EC 2.1.1.34) (tRNA [Gm18] methyltransferase) (Q5SM16)
Organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
Function: Catalyzes the 2'-O methylation of guanosine at position 18 in tRNA. Type I methylase, which methylates all tRNAs.
Interaction partners:
Sequence:
MRERTEARRRRIEEVLRRRQPDLTVLLENVHKPHNLSAILRTCDAVGVLEAHAVNPTGGVPTFNETSGGSHKWVYLRVHPDLHEAFRFLKERGFTVYATALREDARDFREVDYTKPTAVLFGAEKWGVSEEALALADGAIKIPMLGMVQSLNVSVAAAVILFEAQRQRLKAGLYDRPRLDPELYQKVLADWLRK
Protein: WD repeat-containing protein 37 (Q9Y2I8)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:31327510, ECO:0000269|PubMed:34642815}. Nucleus {ECO:0000269|PubMed:31327510}. Note=Primarily localized in the cytoplasm with the highest concentration in the perinuclear region and in small clusters at the leading edge of the spreading cells. {ECO:0000269|PubMed:34642815}.
Interaction partners:
- Phosphofurin acidic cluster sorting protein 1
- Phosphofurin acidic cluster sorting protein 2
Sequence:
MPTESASCSTARQTKQKRKSHSLSIRRTNSSEQERTGLPRDMLEGQDSKLPSSVRSTLLELFGQIEREFENLYIENLELRREIDTLNERLAAEGQAIDGAELSKGQLKTKASHSTSQLSQKLKTTYKASTSKIVSSFKTTTSRAACQLVKEYIGHRDGIWDVSVAKTQPVVLGTASADHTALLWSIETGKCLVKYAGHVGSVNSIKFHPSEQLALTASGDQTAHIWRYAVQLPTPQPVADTSISGEDEVECSDKDEPDLDGDVSSDCPTIRVPLTSLKSHQGVVIASDWLVGGKQAVTASWDRTANLYDVETSELVHSLTGHDQELTHCCTHPTQRLVVTSSRDTTFRLWDFRDPSIHSVNVFQGHTDTVTSAVFTVGDNVVSGSDDRTVKVWDLKNMRSPIATIRTDSAINRINVCVGQKIIALPHDNRQVRLFDMSGVRLARLPRSSRQGHRRMVCCSAWSEDHPVCNLFTCGFDRQAIGWNINIPALLQEK
Protein: Dynein, axonemal, heavy polypeptide 9 (Q7SY17)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MEEQEPLITDKRLDYLENCVLKALNVKPERWERCVSAEEQRRVIQEFLDQSEHSTLSVSVNSTGQLVPALGLSAAVKSKAVFFVKRGKGALTADKMKTQLFSGDMCYSPLEQFSVLVDKVVEPVLSNLNNQRDFPKVVSQDLMRHIHALQNNVFVTAGQIKGKTHLPVPLGFKQFEQCSQQLDKRFHVVDKSLIHSMETVVIDWSHQVYKVLKKDSSEPLLEGRNPTPHAEIQFWRNRLADLQGIQQQLQSSKVLTLAELLLAVDSSYYPAFAKMIQDVMEAHNESKNITTFLKPLERLIEDLENADFTELKAKIPPLMHTVCLIWANCRYYSKPARVIVLLQEICNLLIQQARSFLNPDDILKGDVLESLLRVQAAVDLLTHFKNTYEDRRANLSHYQKNDDPVKPWDFSPLMVFVGLDHFMKRLRTIETVLLTVMDMMRLEKIEFGGIQGKSLSQIVQRLHEDFLQTYKSFSEKPYDCLDVNNMEFESDFAEFQLTVDDTNRRLGAVFCNAFDDASGLEHSFKVLDMFGRLLEQPLIAAEAQARYPVLIKLFDKQLEDCKTIFKKQMQMEETRGYSPVSKNMPAVSGGLKFVQELQERIQTLYNNFRFINHP