wanglab/gogpt-training-data huggingface dataset:
Protein: Cytochrome c oxidase subunit Va (Q5APK5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004434}.
Interaction partners:
- Cytochrome c oxidase subunit
- Cytochrome b-c1 complex subunit 7, mitochondrial
- Cytochrome c oxidase subunit 6, mitochondrial
- Cytochrome c oxidase subunit 8, mitochondrial
- Cytochrome b-c1 complex subunit 8, mitochondrial
- Cytochrome c oxidase subunit 3
- Cytochrome c oxidase subunit 4, mitochondrial
- Cytochrome b-c1 complex catalytic subunit, mitochondrial
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase subunit 1
Sequence:
MFMRSLQRAATKANTASITTSILRFNSTVAKSTSAAPRALSNAYIGNLESRWTSLPKQDQQTLIDELKSRMELPWQELTPAEKKAAYYISFGEWGPRTPLYLPGERSQVFWITTGCIVASVVLFFGIRQFASPPPITMNKEWQEQSDDYLKSKNANPFTGYSQVQ
Protein: Spliceosome-associated protein CWC27 homolog (Probable inactive peptidyl-prolyl cis-trans isomerase CWC27 homolog) (PPIase CWC27) (Q3TKY6)
Organism: Mus musculus (Mouse)
Function: As part of the spliceosome, plays a role in pre-mRNA splicing. Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q6UX04}.
Interaction partners:
- U5 small nuclear ribonucleoprotein 200 kDa helicase
- Pre-mRNA-splicing factor ATP-dependent RNA helicase DHX16
- Pre-mRNA-processing-splicing factor 8
- BUD13 homolog
- Pre-mRNA-processing factor 19
- Splicing factor 3A subunit 3
- 116 kDa U5 small nuclear ribonucleoprotein component
- Pre-mRNA-splicing factor CWC22 homolog
- Ring finger protein 113A1
- Splicing factor 3B subunit 1
Sequence:
MSNIYIQEPPTNGKVLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGTGGESIYGAPFKDEFHSRLRFNRRGLVAMANAGPHDNGSQFFFTLGRADELNNKHTIFGKVTGDTVYNMLRLTEVDIDDEERPRNPHRIKSCEVLFNPFDDITPREIKKPKNEKPEEEVKKLKPKGTKNFSLLSFGEEAEEEEEEVNRVSQSMKGRSKSSHDLLKDDPHLSSVPAVESEKDDATGDLEDDGEDDSAERDEYMEDDEKNLMRERIAKRLKKDASASVKSAGDGEKKPASRSEELRKEARQLKRELLAAKQKKETAIKVEEGREEEEAAPDGAVAEYRREKQKYEALRKQQPKKGTSREDQTLALLSQFKSKLTQAITETPENSVPEAEVEDDEGWMSHVLQFEDKTRKVKDASMQDSDTFEIYDPRNPVNKRRREESKKLLREKKERR
Protein: Peptide ABC transporter, ATP-binding protein (Q88AW9)
Organism: Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000)
Interaction partners:
- Inner membrane ABC transporter permease protein YejB
- Peptide ABC transporter, permease protein
- Bacterial extracellular solute-binding protein, family 5
- ABC-type dipeptide transporter
- ABC-type dipeptide transporter
- Peptide ABC transporter, permease protein
- Inner membrane ABC transporter permease protein YejB
- ABC transporter, permease protein
- Inner membrane ABC transporter permease protein YejB
- ABC transporter, periplasmic substrate-binding protein
Sequence:
MQDNLIEIRDLRVAFNGHEVVHGISLDIRRGECLALVGESGSGKSVTAHSILRLLPPKNVSTQGSIRYDGLDLVTASDKQLRSLRGNRVAMIFQEPMSSLNPLHTVEKQIGEILVTHKGLKGKAALSRTLELLELVGIREPLLRLKAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQVKILELLKSLQQRLNMSLLLISHDLNLVRRIAQRVCVMREGEIVEQADCQALFDNPQHPYSRLLINAEPDGEPVPSTHSNTLLSVQDLKVWFPLGKAWFQREQQYVKAVDGVSFELLKGKTLGIVGESGSGKSTLGQAILRLVDSEGSIRFGTKELSLHSQHLMRPLRRQLQVVFQDPFGSLSPRMTVEQIIAEGLVTHKIGTPKEREQTVIRVLQEVGLDPATRHRYPHEFSGGQRQRISIARALVLEPDLILLDEPTSALDRTVQKQIVALLRDLQIRHGLTYLFISHDLAVVHALAHDLIVIKDGKVVEQGPSREIFAAPQQAYTQELLRSSGLVFA
Protein: Jupiter microtubule associated homolog 2 (Hematological and neurological expressed 1-like protein) (HN1-like protein) (Q9H910)
Organism: Homo sapiens (Human)
Function: Nicotinic acid adenine dinucleotide phosphate (NAADP) binding protein required for NAADP-evoked intracellular calcium release. Confers NAADP-sensitivity to the two pore channels (TPCs) complex. Enables NAADP to activate Ca(2+) release from the endoplasmic reticulum through ryanodine receptors.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15094197, ECO:0000269|PubMed:33758062}. Nucleus {ECO:0000269|PubMed:15094197}. Note=Colocalizes with type 1 ryanodine receptor (RYR1). {ECO:0000269|PubMed:33758062}.
Interaction partners:
- Jupiter microtubule associated homolog 1
Sequence:
MFQVPDSEGGRAGSRAMKPPGGESSNLFGSPEEATPSSRPNRMASNIFGPTEEPQNIPKRTNPPGGKGSGIFDESTPVQTRQHLNPPGGKTSDIFGSPVTATSRLAHPNKPKDHVFLCEGEEPKSDLKAARSIPAGAEPGEKGSARKAGPAKEQEPMPTVDSHEPRLGPRPRSHNKVLNPPGGKSSISFY
Protein: Chromodomain helicase DNA binding protein 3 (A0A5F8MQ82)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
KREDVKADRELRLGPPRDEPRPNGRREEKVEKPRFMFNIADGGFTELHTLWQNEERAAISSGKLNEIWHRRHDYWLLAGIVLHGYARWQDIQNDAQFAIINEPFKTEANKGNFLEMKNKFLARRFKLLEQALVIEEQLRRAAYLNLSQEPAHPAMALHARFAEAECLAESHQHLSKESLAGNKPANAVLHKGKGRGGPARGRAHNAASEPAGGIAERHEGRCDPPASHAVPNTPHRSPPSDVRAQHPQPAGQQGHGASPHTGLSPGSLRHTSGVRGSLQRRTRRGPGRRRRQLQPDACRVLHHSHHQRPSSAGEEREGNGGGVGIRRAGAGSEGAPSRGGDLYRRLTGSQACPSPRPRPRSRPTSQALGPVANPPPSPPLGPPLG
Protein: GDP-L-fucose synthase (EC 1.1.1.271) (GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase) (P32055)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the two-step NADP-dependent conversion of GDP-4-dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction.
Subcellular location: Cytoplasm.
Interaction partners:
- GDP-mannose 4,6-dehydratase
- GDP-mannose mannosyl hydrolase
- Putative colanic acid biosynthesis glycosyl transferase WcaI
- UDP-glucose:undecaprenyl-phosphate glucose-1-phosphate transferase
- Putative colanic acid biosynthesis acetyltransferase WcaF
- Putative colanic acid biosynthesis glycosyl transferase WcaE
- Mannose-1-phosphate guanylyltransferase
- Putative colanic acid biosynthesis glycosyl transferase WcaC
- Putative polysaccharide export protein Wza
- Phosphomannomutase
Sequence:
MSKQRVFIAGHRGMVGSAIRRQLEQRGDVELVLRTRDELNLLDSRAVHDFFASERIDQVYLAAAKVGGIVANNTYPADFIYQNMMIESNIIHAAHQNDVNKLLFLGSSCIYPKLAKQPMAESELLQGTLEPTNEPYAIAKIAGIKLCESYNRQYGRDYRSVMPTNLYGPHDNFHPSNSHVIPALLRRFHEATAQNAPDVVVWGSGTPMREFLHVDDMAAASIHVMELAHEVWLENTQPMLSHINVGTGVDCTIRELAQTIAKVVGYKGRVVFDASKPDGTPRKLLDVTRLHQLGWYHEISLEAGLASTYQWFLENQDRFRG
Protein: Pectinesterase inhibitor 12 (Pectin methylesterase inhibitor 12) (OsPMEI12) (Q10T67)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Pectin methylesterase (PME) inhibitor that inhibits PME in vitro.
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000269|PubMed:26874295}.
Interaction partners:
- Small ribosomal subunit protein uS9
- Small ribosomal subunit protein eS19
- 40S ribosomal protein S29, putative, expressed
- Os10g0411700 protein
- Os01g0220300 protein
- 40S ribosomal protein S30
- 40S ribosomal protein S15, putative, expressed
- Small ribosomal subunit protein uS19
- 40S ribosomal protein S12
- 40S ribosomal protein S21
Sequence:
MRMSKALAAVVAISVSLSAAAMGVDATVESTCSDAAASDKRVHLAMCLSQLGHHRDADAWGLAKAATLVGVDKADLAADDIKELEAGASTAGIKPALAECAKQYRGVGFAFASAHDVINNRAYDVGEKKLDEALSLTQKCNAAFAKIGVPLQQPLAQLTADTIQIAIIAKAITCLVNVNNNPALVAAAAAAAAAKAPQQSQYP
Protein: Methylenetetrahydrofolate reductase (NADH) 2 (AtMTHFR2) (EC 1.5.1.54) (O80585)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The probable reversibility of the MTHFR reaction in plants suggests that they can metabolize the methyl group of 5,10-methylenetetrahydrofolate to serine, sugars and starch.
Interaction partners:
- Bifunctional dihydrofolate reductase-thymidylate synthase
- Aminomethyltransferase, mitochondrial
- Serine hydroxymethyltransferase 1, mitochondrial
- Bifunctional dihydrofolate reductase-thymidylate synthase 1
- Bifunctional dihydrofolate reductase-thymidylate synthase 2
- Serine hydroxymethyltransferase 2, mitochondrial
- Serine hydroxymethyltransferase 4
- Serine hydroxymethyltransferase 5
- Serine hydroxymethyltransferase 7
- Serine hydroxymethyltransferase 6
Sequence:
MKVIDKIQSLADEGKTAFSFEFFPPKTEDGVDNLFERMDRMVAYGPTFCDITWGAGGSTADLTLDIASRMQNVVCVESMMHLTCTNMPVEKIDHALETIRSNGIQNVLALRGDPPHGQDKFVQVEGGFDCALDLVNHIRSKYGDYFGITVAGYPEAHPDVIGENGLASNEAYQSDLEYLKKKIDAGADLIVTQLFYDTDIFLKFVNDCRQIGISCPIVPGIMPINNYRGFLRMTGFCKTKIPVEVMAALEPIKDNEEAVKAYGIHLGTEMCKKMLAHGVKSLHLYTLNMEKSALAILMNLGMIDESKISRSLPWRRPANVFRTKEDVRPIFWANRPKSYISRTKGWEDFPQGRWGDSRSASYGALSDHQFSRPRARDKKLQQEWVVPLKSVEDIQEKFKELCLGNLKSSPWSELDGLQPETRIINEQLIKVNSKGFLTINSQPSVNAERSDSPTVGWGGPVGYVYQKAYLEFFCSKEKLDAVVEKCKALPSITYMAVNKGEQWVSNTAQADVNAVTWGVFPAKEIIQPTIVDPASFNVWKDEAFETWSRSWANLYPEADPSRNLLEEVKNSYYLVSLVENDYINGDIFAVFADL
Protein: Peroxisomal coenzyme A diphosphatase ndx-8 (EC 3.6.1.-) (Nudix hydrolase 8) (Q9NA25)
Organism: Caenorhabditis elegans
Function: Coenzyme A diphosphatase which mediates the cleavage of CoA into 3',5'-ADP and 4'-phosphopantetheine.
Subcellular location: Peroxisome membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MKCVVSRADDLKRMLDLSDVPTKSQGEQDAGVLILLHDDGSEKLKVLLCVRSRQLRRHPGEVCFPGGMMDDEDGQNVRRTAIREAYEEVGVNENDDYLVLGNLPAFRARFGVLIHPTVALLRRPPTFVLSIGEVESIFWIPLSQFLEDTHHSTFLIDEFYMVHVFQFDEYPTTYGVTALMCIVVAIGLLGKLPNFNLMGNLTISDMLDKHLDSIEIIRHVYEFASRKFEPKSKI
Protein: Ubiquitin-conjugating enzyme E2, putative (EC 6.3.2.19) (Q38EF6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Nonspecific lipid-transfer protein, putative
- propanoyl-CoA C-acyltransferase
- Ubiquitin-protein ligase, putative
- Ubiquitin-protein ligase, putative
- E3 ubiquitin-protein ligase TRIP12
- HECT-type E3 ubiquitin transferase
- Ubiquitin-conjugating enzyme, putative
- Polyubiquitin, putative
- Anaphase-promoting complex subunit 11
- Ubiquitin thioesterase
Sequence:
MTLTPRIIKETEKMRKDPPEGITATPSPENPRHFHVTIRGPPQSSYEGGIFELELFLPEEYPMVPLKVRFLTRIYHPNVDKLGRICLDVIKDKWSPALQIAQVLLSIQLLMASPNPDDPLDNEVAGAWKRNEAEAMKVAREWTKKYANKA
Protein: Unconventional prefoldin RPB5 interactor 1 (Protein NNX3) (Protein phosphatase 1 regulatory subunit 19) (RNA polymerase II subunit 5-mediating protein) (RPB5-mediating protein) (O94763)
Organism: Homo sapiens (Human)
Function: Involved in gene transcription regulation. Acts as a transcriptional repressor in concert with the corepressor UXT to regulate androgen receptor (AR) transcription. May act as a tumor suppressor to repress AR-mediated gene transcription and to inhibit anchorage-independent growth in prostate cancer cells. Required for cell survival in ovarian cancer cells. Together with UXT, associates with chromatin to the NKX3-1 promoter region. Antagonizes transcriptional modulation via hepatitis B virus X protein.
Subcellular location: Nucleus. Cytoplasm. Mitochondrion. Cell projection, dendrite {ECO:0000250}. Note=Colocalizes with PFDN2, PFDN4, PPP1CC, RPS6KB1 and STAP1 at mitochondrion.
Interaction partners:
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- Prefoldin subunit 2
- Protein UXT
- RuvB-like 1
- Prefoldin subunit 6
- RuvB-like 2
- RNA polymerase II-associated protein 3
- p53 and DNA damage-regulated protein 1
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Dynein axonemal assembly factor 10
Sequence:
MEAPTVETPPDPSPPSAPAPALVPLRAPDVARLREEQEKVVTNCQERIQHWKKVDNDYNALRERLSTLPDKLSYNIMVPFGPFAFMPGKLVHTNEVTVLLGDNWFAKCSAKQAVGLVEHRKEHVRKTIDDLKKVMKNFESRVEFTEDLQKMSDAAGDIVDIREEIKCDFEFKAKHRIAHKPHSKPKTSDIFEADIANDVKSKDLLADKELWARLEELERQEELLGELDSKPDTVIANGEDTTSSEEEKEDRNTNVNAMHQVTDSHTPCHKDVASSEPFSGQVNSQLNCSVNGSSSYHSDDDDDDDDDDDDDNIDDDDGDNDHEALGVGDNSIPTIYFSHTVEPKRVRINTGKNTTLKFSEKKEEAKRKRKNSTGSGHSAQELPTIRTPADIYRAFVDVVNGEYVPRKSILKSRSRENSVCSDTSESSAAEFDDRRGVLRSISCEEATCSDTSESILEEEPQENQKKLLPLSVTPEAFSGTVIEKEFVSPSLTPPPAIAHPALPTIPERKEVLLEASEETGKRVSKFKAARLQQKD
Protein: Mitogen-activated protein kinase (EC 2.7.11.24) (B4LQZ8)
Organism: Drosophila virilis (Fruit fly)
Interaction partners:
- mitogen-activated protein kinase kinase
- non-specific serine/threonine protein kinase
- Uncharacterized protein
- Mothers against decapentaplegic homolog
- non-specific serine/threonine protein kinase
- Uncharacterized protein, isoform A
- Mothers against decapentaplegic homolog
- Rap-GAP domain-containing protein
- Importin N-terminal domain-containing protein
- Forkhead box protein O
Sequence:
MAEGNTGTSAEGAAALAAPHPNAEVIRGQIFEVGPRYRKLTYIGEGAYGMVVSADDTLTNQRVAIKKISPFEHQTYCQRTLREITILTRFKHENIIDIRDILRVDSIEQMRDVYIVQCLMETDLYKLLKTQRLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNKTCDLKICDFGLARIADPEHDHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILGVLGSPSQEDLECIINEKARNYLESLPFKPNVPWSRLFPNADALALDLLGKMLTFNPHKRIPVEEALAHPYLEQYYDPGDEPVAEVPFRINMENDDISRDALKSLIFEETLKFKERQPEQAL
Protein: V-type proton ATPase 21 kDa proteolipid subunit c'' (V-ATPase 21 kDa proteolipid subunit c'') (23 kDa subunit of V-ATPase) (Vacuolar proton pump 21 kDa proteolipid subunit c'') (Q91V37)
Organism: Mus musculus (Mouse)
Function: Proton-conducting pore forming subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity).
Subcellular location: Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250|UniProtKB:Q2TA24}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- V-type proton ATPase subunit S1
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase subunit E 1
- V-type proton ATPase subunit D
- V-type proton ATPase 116 kDa subunit a 1
- V-type proton ATPase subunit d 1
- Renin receptor
- V-type proton ATPase subunit B, brain isoform
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit H
Sequence:
MTGLELLYLGIFVAFWACMVVVGICYTIFDLGFRFDVAWFLTETSPFMWSNLGIGLAISLSVVGAAWGIYITGSSIIGGGVKAPRIKTKNLVSIIFCEAVAIYGIIMAIVISNMAEPFSATEPKAIGHRNYHAGYSMFGAGLTVGLSNLFCGVCVGIVGSGAALADAQNPSLFVKILIVEIFGSAIGLFGVIVAILQTSRVKMGD
Protein: Mimecan (Osteoglycin) (Q62000)
Organism: Mus musculus (Mouse)
Function: Induces bone formation in conjunction with TGF-beta-1 or TGF-beta-2.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q8MJF1}.
Interaction partners:
- Osteomodulin
- Lumican
- Fibromodulin
- Asporin
- Prolargin
- Keratocan
- Decorin
- Aggrecan core protein
Sequence:
METVHSTFLLLLFVPLTQQAPQSQLDSHVNYEYATGNSEETKFSQDYEDKYLDGKSIKEKETMIIPDEKSLQLQKDEVIPSLPTKKENDEMPTCLLCVCLSGSVYCEEVDIDAVPPLPKESAYLYARFNKIKKLTAKDFADMPNLRRLDFTGNLIEDIEDGTFSKLSLLEELTLAENQLLRLPVLPPKLTLLNAKHNKIKSKGIKANTFKKLNKLSFLYLDHNDLESVPPNLPESLRVIHLQFNSISSLTDDTFCKANDTRYIRERIEEIRLEGNPIALGKHPNSFICLKRLPIGSYF
Protein: Polymerase acidic protein (EC 3.1.-.-) (RNA-directed RNA polymerase subunit P2) (P31343)
Organism: Influenza A virus (strain A/Victoria/3/1975 H3N2)
Function: Plays an essential role in viral RNA transcription and replication by forming the heterotrimeric polymerase complex together with PB1 and PB2 subunits. The complex transcribes viral mRNAs by using a unique mechanism called cap-snatching. It consists in the hijacking and cleavage of host capped pre-mRNAs. These short capped RNAs are then used as primers for viral mRNAs. The PB2 subunit is responsible for the binding of the 5' cap of cellular pre-mRNAs which are subsequently cleaved after 10-13 nucleotides by the PA subunit that carries the endonuclease activity.
Subcellular location: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04063}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04063}. Note=PB1 and PA are transported in the host nucleus as a complex. {ECO:0000250|UniProtKB:P03433, ECO:0000255|HAMAP-Rule:MF_04063}.
Interaction partners:
Sequence:
MEDFVRQCFNPMIVELAEKAMKEYGEDLKIETNKFAAICTHLEVCFMYSDFHFINEQGESIVVELDDPNALLKHRFEIIEGRDRTMAWTVVNSICNTTGAEKPKFLPDLYDYKENRFIEIGVTRREVHIYYLEKANKIKSENTHIHIFSFTGEGMATKADYTLDEESRARIKTRLFTIRQEMANRGLWDSFRQSERGEETIEERFEITGTMRRLADQSLPPNFSCLENFRAYVDGFEPNGCIEGKLSQMSKEVNAKIEPFLKTTPRPIKLPDGPPCFQRSKFLLMDALKLSIEDPSHEGEGIPLYDAIKCMRTFFGWKEPYIVKPHERGINSNYLLSWKQVLAELQDIENEEKIPRTKNMKKTSQLKWALGENMAPEKVDFDNCRDISDLKQYDSDEPELRSLSSWIQNEFNKACELTDSIWIELDEIGEDVAPIEYIASMRRNYFTAEVSHCRATEYIMKGVYINTALLNASCAAMDDFQLIPMISKCRTKEGRRKTNLYGFIIKGRSHLRNDTDVVNFVSMEFSLTDPRLEPHKWEKYCVLEIGDMLLRSAIGQMSRPMFLYVRTNGTSKIKMKWGMEMRRCLLQSLQQIESMIEAESSVKEKDMTKEFFENKSETWPIGESPKGVEEGSIGKVCRTLLAKSVFNSLYASPQLEGFSAESRKLLLVVQALRDNLEPGTFDLGGLYEAIEECLINDPWVLLNASWFNSFLTHALR
Protein: Helix-loop-helix DNA-binding domain containing protein (Q2QLR0)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDDSSFFMQWAMDTLHQLPSDSTAAAAYATDVAGDSGAFPSLQALRNASAAGGGGGFRDLTVQVDQVHRANSWSSSDSPGGGAATAAAGWSPHVTGGGGRGHRPMSWNFSAASAQPTTEDSGGGGGGGVVPAPLQAMETTATARAAVKKGGGGGSSSSAAAPGYVQDHIIAERRRREKINQRFIELSTVIPGLKKMDKATILGDAVKYVKELQEKVKTLEEEDGGGRPAAMVVRKSSCSGRQSAAGDGDGEGRVPEIEVRVWERSVLVRVQCGNSRGLLVRLLSEVEELRLGITHTSVMPFPASTVIITITAKASSLSNHPALLCLYICIKLPCVISS
Protein: Exotoxin A regulatory protein (P09852)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Positive regulation of toxA gene transcription.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:2105298}; Peripheral membrane protein {ECO:0000269|PubMed:2105298}.
Interaction partners:
- Exotoxin A
- HTH-type transcriptional regulator PtxR
- Sigma factor PvdS
- Uncharacterized protein
- Acetylpolyamine amidohydrolase 2
Sequence:
MTATDRTPPPLKWLCLGNRDANDGFELFAHGIYARNGALVGSKLSLRERRQRVDLSAFLSGAPPLLAEAAVKHLLARLLCVHRHNTDLELLGKNFIPLHASSLGNAGVCERILASARQLQQHQVELCLLLAIDEQEPASAEYLTSLARLRDSGVRIALHPQRIDTDARQCFAEVDAGLCDYLGLDARLLAPGPLTRNLRQRKSIEYLNRLLVAQDIQMLCLNVDNEELHQQANALPFAFRHGRHYSEPFQAWPFSSPAC
Protein: Mitochondrial transcription termination factor family protein (Q3ED83)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSSLLHCRNVVDCAFTSSTVRRIVNLGFLVGRIRTLCSVSQVKSENLEKQKPCLESFTVSYLVDSCGLSLESAKSNSRFVKLVSSKKPDSVLALFKDHGFTNDQITSVIKSFPRVLSLSPEDVISPKLMFFSSIGFSTSDTAKMISSSPKMLSYSLHKRLIPCYDSLKSILVEEESVVKCLKRGIRCFSLKITHCVSLRVSICRELGVPDKSIKWLVQASPFTFFSRERRFNEVLNRVCSYGFDPKKAGFVHAMVAFDCTSESAMERKFKLFQCFGWSKEDFVAAIMRFPNCVTVSDEKIMYTLEYLVNNIGLQARDIVARPVVLSLSMEKRIKPRNQVISLLLSKGLVKKEDINYFTILKLKSSEFMDKFVLKYQDEMPQLVQPFTSNR
Protein: Stromal cell-derived factor 2-like 1 (D4A9Y0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- DnaJ homolog subfamily B member 11
- Endoplasmin
- Protein disulfide-isomerase A4
- Sorting nexin-5
- Hypoxia up-regulated protein 1
- Protein disulfide isomerase Creld2
- Endoplasmic reticulum chaperone BiP
- Peptidyl-prolyl cis-trans isomerase B
- DnaJ homolog subfamily C member 10
- Protein disulfide-isomerase A6
Sequence:
MLGASRGLAGLTLLGLLLALSVRSGGASKASAGLVTCGSVLKLLNTHHRVRLHSHDIKYGSGSGQQSVTGVEASDDANSYWRIRGGSEGGCPRGLPVRCGQAVRLTHVLTGKNLHTHHFPSPLSNNQEVSAFGEDGEGDDLDLWTVRCSGQHWEREASVRFQHVGTSVFLSVTGEQYGNPIRGQHEVHGMPSANAHNTWKAMEGIFIKPGADPSTGHDEL
Protein: Acetyl-CoA acetyltransferase, mitochondrial (EC 2.3.1.9) (Acetoacetyl-CoA thiolase) (T2) (P24752)
Organism: Homo sapiens (Human)
Function: This is one of the enzymes that catalyzes the last step of the mitochondrial beta-oxidation pathway, an aerobic process breaking down fatty acids into acetyl-CoA. Using free coenzyme A/CoA, catalyzes the thiolytic cleavage of medium- to long-chain 3-oxoacyl-CoAs into acetyl-CoA and a fatty acyl-CoA shortened by two carbon atoms. The activity of the enzyme is reversible and it can also catalyze the condensation of two acetyl-CoA molecules into acetoacetyl-CoA. Thereby, it plays a major role in ketone body metabolism.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:1979337}.
Interaction partners:
- Hydroxymethylglutaryl-CoA synthase, cytoplasmic
- Hydroxymethylglutaryl-CoA synthase, mitochondrial
- Trifunctional enzyme subunit alpha, mitochondrial
- Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial
- Succinyl-CoA:3-ketoacid coenzyme A transferase 2, mitochondrial
- Enoyl-CoA delta isomerase 2
- Peroxisomal bifunctional enzyme
- Citrate synthase, mitochondrial
- Hydroxymethylglutaryl-CoA lyase, mitochondrial
- Peroxisomal acyl-coenzyme A oxidase 1
Sequence:
MAVLAALLRSGARSRSPLLRRLVQEIRYVERSYVSKPTLKEVVIVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYKRVDFSKVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQGEYGLASICNGGGGASAMLIQKL
Protein: Dynein axonemal intermediate chain 1 (Axonemal dynein intermediate chain 1) (Q8C0M8)
Organism: Mus musculus (Mouse)
Function: Part of the dynein complex of respiratory cilia.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q9UI46}.
Interaction partners:
- Dynein axonemal heavy chain 5
- Thioredoxin domain-containing protein 3
- Dynein axonemal heavy chain 11
- Outer dynein arm-docking complex subunit 1
- Dynein, axonemal, heavy chain 10
- Dynein axonemal intermediate chain 2
- Dynein, axonemal, heavy chain 9
- Dynein, axonemal, heavy chain 6
- Dynein axonemal heavy chain 1
- Dynein axonemal heavy chain 8
Sequence:
MPSKQIRKQSISVTRGARRRDEDSGTDVGEGTDEWSQSKATVRPPDQLELTDAELKEEFTRILTANNPHAPQNIVRYSFKEGTYKLIGFVNQMAVHFSQVGNLIPKDSDEGRRQHYRDEMVAGSQESIKVVTSEAENLEEEEEPKEGEGEAEAEAEAGSQTDIPAAAETTEKVIEEELMAPVQPKERKLTNQFNFSERASQTFNNPLRDRECQMEPPPRTNFSATANQWEIYDAYVDELEKQEKTKEKEKAKTPVAKKTEKMAMRKLTSMESQSDDITKVTQAAKIVERMVNQNTYDDVAQDFKYYEDTADEYRDQEGTLLPLWKFQNDKAKRLAVTALCWNPKYKDLFAVGHGSYDFMKQSRGMLLLYSMKNPSFPEYMFSSESGIMCLDVHVDHPYLVVVGYYDGNVAIYNLKKPHSQPCFRSTSKSGKHTDPVWQVKWQKDDMDHNLNFFSVSSDGRIVSWTLVKSELVHIDIIKLKTEGSTTEIPEGLQLHTVGCGTAFDFHKEIDYMFLVGTEEGKIYKCSKSYSSQFLDTYDAHNMAVDAVLWNPYHTKVFMSCSSDWTVKIWDHTIKTPMFIYDLNSAVGDVAWAPYSSTVFAAVTTDGKAHVFDLAVNKYEAICNQPVVAKKKNKITHVQFNPIHPIIIVGDDRGHIICLKLSPNLRKMPKEKKGQEVQKGPAVEIAKLDKLLNLVREVKTKT
Protein: Ecdysone-inducible gene E1 (Q9VSJ0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTATARQSATSRKQPAIAMLNGNAFTVKRLLALLIIFTVVDASRSLELGDKCQHDMDCTDFIKGSSCSALGYCECAPYFVQLDSKRCLSSQLLGGDCQLSEQCSMKVANSSCLEGACRCVEGFLQFRKHTCLGPAHPGAVCYSHAHCQMFDTRTHCDFLIPNLFGRCQCTSPAKMVGGLCVAPAADQEDQKQEQAVEKVEQPASSTTTTTTTTTTPRPTTRTTSRTTTTTTAAPPTTTRRTTTTTTTTTPAPILLEDELPASVEEQSLEEDDGETTKLRPEVVEVDNGEKLEAVDLAHEETELTQQQNQLDEQQHQEEEQKHQEEEQHRIEQQQNQEEEQQQQQHQQQVIDQASDAELPQSSQDATTGVQQLLTPADVPTEDAINAEQETEAGPTEDYPYKIDEEYTEEHNDKPEAPELTVDQPEHEESPVATEIVPIEADEEAAEASGGQEIASSPIDDTMKFDYETSVDDVEPAKPEDEKETEAVHQATNEGVVPIDTESETDAETSTEPQIQTQLLQEDGEPETSQTVADEELIPVNEGETESVTKAADETEEIPEEETPEDLASGDHELDVAAASHDDEVETPKQEEPTEALKIEQPAQVESESQNVDEVGKPEEPQAEMEIEKEKEETAATEAAEVELPATEAKPDMESEIDQVEQSADIKPTSGEDDLNEANQLNQDQVTEPAALEQEEIEEKEPEQVVDMHEDADEATTEKPVQDHDQEEVEAITEAEHGQLTYPTNDDELAPVEIEPELTTEEPEIAENTTELPEQQQQQQDEEEIEEAALAHEEQVQQVEPEENANAIKTPEVSEAIAEPQADLETPSATEKEIEPQTADHVEEEPVAITERIQEADPEPEIEPTNDEVSQVDADQAEPELPIKSDADIAKEAAEEPAQTEVAPEVETETEASESAQTSPEISVEQDEVAIDKNENDNIIQGAEPNEEDELIPEPQPMPEEEELPVQQEASAVPEDHKLTKPEMDYTSVEHLQELSRPEETTAAIEAEESDSRESTLAPEAPDAPIAIVSEERDPEHDPQNFHESESIGDILSDLMLEADSTVPPVPFGQQPAQTVPMVEANSENEEEQAHEAISDLQAEADETQEHAEQVQPVNEPGTAIPELFAEAAKDEEDVPALSESDESKTEQPSALEEELHIPSEAEQTPVEDEHQYDEEEHQQDQEEHQQDEDEPLKEVETESLPEEATTEKFQEPEPEEVNTPLPEELPFDLTDHSDVNRFNELQSESLILESTTNIDGLQELDNNHIEEEEPAAHAIPHEEATPNPADIVEITTQTMLGLASRVTLMEPAAPVVTTLMPLMTADEPTPEPVSPAAIPSASLAAIKPGTELRKRVDLGLEAVSLGLACSSDRQCQLADPHTVCNRRGVCDCAAGEEGSQCSAERTGCSPGTFQCRSSGVCISWFFVCDGRADCNDASDEECTHNARLNQTCPTESFRCQRSGRCISRAALCDGRRQCPHGEDELGCDGSVKGGNACPEHTFRCGSGECLPEYEYCNAIVSCKDGSDEPPHLCGSRALPNLFMRLIEAGGLLGGGRREADAYCPHRCSNGLCRSTAIVCSGRDGCGDGTDEQTCSVCRCPAPTAASLPAFLARQRPMPLW