wanglab/gogpt-training-data huggingface dataset:
Protein: EngB-type G domain-containing protein (Q380Y8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- GTP-binding protein, putative
- GTP-binding protein, putative
- tRNA/rRNA methyltransferase SpoU type domain-containing protein
- Large ribosomal subunit protein bL21m
- Uncharacterized protein
- 50S ribosomal protein L17, putative
- 50S ribosomal protein L14, putative
- 50S ribosomal protein L13, putative
- Acyl carrier protein
- Pseudouridylate synthase RPUSD4, mitochondrial
Sequence:
MCICTRLLCCSGIGQARRQLTPASSRQKPWGNDPPHLMSPQDELVAKLSDEVFSRGNMHLKNVDVVSALPEGLHSFPEVCFIGKPNVGKSSIISCLLRNPRLGRAGRVRGTTRLLQFFNVGDALLLVDTPGYGGWKGRHLPQSVAERASAFAILFRYLALRSKGPLKRVYWVMEATKPVQPRDEEIFVFLRNEQIPFSIIISKLDYFGGDGAALRRQVESIYNFLGTEDVPVLGVRADSSRPERCINMTALQHDITHYCTTDLVRVEDLSYNGLKELSYAPPTFDEVRAVEERYPVESFIVPQDDNLSLQHFVSLHQEAKSRHLTTSPMAMRLSTKEKLGANLIGDDGGSKGIDIDEGTIVAHSPLLARLTIAAEGTIPDSSLLEGVPLGVVAVSPTKMPQCFHEHPSIREGLLRTSRVGHTDLQQEEAVNRVQPVSPCPSPTIKHKSSEHLSCKPTGSLGGDAPGAPPFSPSRFGAHMETIRTINGVCIPKSMVPPSVVQLAAGQAGSFAAFAQHSGANAYEEFLTGDATGSGTFLEATGSEDTLENKGRSLRRPREKSMRRCALDKVLKRYVACGRKQRSLHMQAEGYMCPWLAGAGQQARSAVFGVTRSRAHAGGMEVLKGLKRTGFGGQSYSARTMKNRGRSTKKTGFWAA
Protein: AhpC/TSA family protein (Q8YP05)
Organism: Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
Interaction partners:
- Thioredoxin reductase
- Peroxiredoxin 2 family protein/glutaredoxin
- sulfiredoxin
- GTPase HflX
- Thioredoxin
- Thioredoxin 1
- thioredoxin-dependent peroxiredoxin
- Thioredoxin
- Alr4642 protein
- Thioredoxin 2
Sequence:
MALRLGDTVPNFTQASTHGDIDFYAWAGDSWVVLFSHPADYTPVCTTELGTVAKLKPEFDKRNVKAIALSVDDVESHNGWVGDIEETQSTTLNYPILADADRKVSDLYDMIHPNANAAVTVRSVFVIDPNKKLRLTFTYPPSTGRNFDELLRVIDSLQLTDNYSVATPADWKDGDKVVIVPSLKDPEVLKEKFPKGYEVVKPYLRLTPQPNK
Protein: Phosphopantetheine adenylyltransferase (EC 2.7.7.3) (Dephospho-CoA pyrophosphorylase) (Pantetheine-phosphate adenylyltransferase) (PPAT) (P0A6I6)
Organism: Escherichia coli (strain K12)
Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. CoA is not a substrate for the enzyme.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00151}.
Interaction partners:
- Coenzyme A biosynthesis bifunctional protein CoaBC
- Dephospho-CoA kinase
- Pantothenate kinase
- 3-deoxy-D-manno-octulosonic acid transferase
- Acyl carrier protein phosphodiesterase
- Bifunctional riboflavin kinase/FMN adenylyltransferase
- Ribosomal RNA small subunit methyltransferase D
- Tetraacyldisaccharide 4'-kinase
Sequence:
MQKRAIYPGTFDPITNGHIDIVTRATQMFDHVILAIAASPSKKPMFTLEERVALAQQATAHLGNVEVVGFSDLMANFARNQHATVLIRGLRAVADFEYEMQLAHMNRHLMPELESVFLMPSKEWSFISSSLVKEVARHQGDVTHFLPENVHQALMAKLA
Protein: Translationally-controlled tumor protein homolog (TCTP) (Q8I3Z5)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Involved in calcium binding and microtubule stabilization.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Small ribosomal subunit protein eS30
- Small ribosomal subunit protein eS1
- 40S ribosomal protein S3
- Elongation factor 1-delta, putative
- Elongation factor 1-beta
- 40S ribosomal protein S8
- 60S acidic ribosomal protein P0
- 60S ribosomal protein L11a, putative
- 40S ribosomal protein S6
- Small ribosomal subunit protein uS2
Sequence:
MKVFKDVFTNDEVCSDSYVQQDPFEVPEFREIAFEVKSNKRIKGNEDYGIADNSEDAVEGMGADVEHVIDIVDSFQLTSTAFSKKEYSAYIKNYMQKVAKYLEEKKPDRVEIFKTKAQPFIKHILTNFDDFEFYMGESLDMEAGIIYSYYKGEEITPRFVYISDGLFEEKY
Protein: Prosap, isoform E (A0A0B4LF25)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSGSGAFDDEPPPEPRDGWLLVRIHVPELNVYKCLQFPSERLVWDVKQQVLASLPKELKESFNYGLFAPPANGKAGKFLDEERRLGDYPFNGPVGYLELKYKRRVYKMLTLDERQLKALHTRANLRRFLECINGGHVEKIAKMCAKGLDPNFHCSESGDTPLTVATGAKKPNKLLIALVNGGALLDYRTKDGSTALHRAVEHDSLEAVSTLLELGASPNYRDGRGITPLYISITRKCEAKITESLLHDHATLGIQDSQGWNEVHQVAVIAGNLELAEIIENYKSEDIDKSLGDTSDIISDSSGVGTNSDSAACSIGHPSTTVVCMEPYAGNTVGHIRLQPGDVIEVVGSTDCGLLEGYVRGTNQSGFFPADCVQEVSLRQKHITNVMTASTGMAPQQQQQQHLQQAPAGSSAASYQGSPQLSLGGHSGSSSTLLQQPHQSPSLSVASNGSCQQPLESNEGGASGNGINNRNNNHSVGQYSSATAPRIKKSAYNAPRSVVLHRAKRGFGFILRGAKASSQLMQLRPSERFPALQYLDDVDPGGVADMAGLRPGDFLLTINGEDVTSASHEQVVEMIRSAGALVNLTVVSPQFPHQMQASAQYLPSGARAGSHHLNSGPSTPQSSHRQCATLPRKMTGPGGSGPGSSSGGSVRMAPMPPRRDPKTTLSVGRARAKSMVAGLENGGEKEDDLPHTKSNSVESIATPTPTGIQTGPGTPVQLRTASIKARPTSSRITAAELEELFQRQQGEGSAANASRYATMMTSSRFQSGTDSGAATPPASNGSPMRSGPLVYGSVAEMKRKTARSKHGSGTLRGKPVATPTVGPGGAGGGRDLKRFHSTPDLHGPQLHGSASSIWQASGKGHHSQDDVATLHASLQRLNSNQGELKLGGLGAGSATGAGGAVLPPPNHPPPPPPVGQVVKVETRSSVSEYESTISLQQKLKKRTENDAVTSAAIDGVQSSFNPSANAKIYASPQELRNVMAWKLRQAQEKPSQETSAGSQQPVSQYAAPTQMRPAQQQQQAQQPPTALASHYAAPQVQVQQVQQVQQSPQQSAPQSPPAPPLPQAAPVPAQNGNGNGSTSGAGSAPPIPEPDYSCSESDGEDENSILVARNTKLNEKIALFDVPETSGNSQASGSSSNSGSASISHSLSVEEIQRIRSNLKTSKSSPNGFAKKPEEEKPQQEQQQSHQQPQQLLQPGEDECDNSSSGVSSEQEQLALAAGVTLPGGGKPTDTIKKKPSVTIVEEPKTIPDQPSSNTSHTTKPMAKTTISIGGGGSAVPTATLTVKQLVQQQHAPVIQQQQQQLGSKQPVTAASTNKFTQQSNINSNVMSPQVLGRIPSHHHQQQSSNPNQKLIATQQQILQQQQQQLAHQQHLQQILKAKAAAAGGASNTAVLVAKHQQKLHKGTSSGHESEMETRSDLEDDDGDLSPSPPAKAFQRHNSLTRKQAAAIAMQRGATRTTAVSLMQLPPPLEADSDGEPSQLTLQRQQSHHPSQTHPHPHQLQQQLQLQQQQQQQQQQQQPMAAHIVGMLPSGQLVAVASGAVAGVPGVGATAVQQGNNNLQQLCTDNLVLAPPPQFCDCNDAKHAPQPHLPTSQYHPQQQQQQQHQQQQQQQQQLQQQLQQQQMLQMHQRLSGGAGAGAVGTLGRVRIVGAMPKANHHRLH
Protein: Dolichol phosphate-mannose mannosyltransferase (EC 2.4.1.-) (Archaeal glycosylation protein S) (D4GYH0)
Organism: Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii)
Function: Involved in the assembly of a N-linked pentasaccharide that decorates the S-layer glycoprotein and flagellins. Transfers mannose, the terminal pentasaccharide residue, from its dedicated dolichol phosphate carrier to the protein-bound glycan comprising the first four subunits of the N-linked pentasaccharide.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23086206}; Multi-pass membrane protein {ECO:0000269|PubMed:23086206}.
Interaction partners:
- Large ribosomal subunit protein eL32
- UTP--glucose-1-phosphate uridylyltransferase AglF
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein uL30
- Glycosyltransferase AglI
- Large ribosomal subunit protein eL18
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein uL22
- Large ribosomal subunit protein uL2
- Large ribosomal subunit protein eL21
Sequence:
MKRLAKAAFSQNSLTAPIVSTFVYLISVVRVVLNGNWPVTSSDTAMFQHIGWMVFSGKRYYIDAWDPKPPLTLELATIIAYISNGDPHLQHTLSVVSTIVAGILLTYLISHITSEITGNQFAGLLSGIVFITFPVIHYSAVFGYEPKYFVFLFGLGSIYLSRNPKPILSGAAAAASAGMWQFAIIFPIISFGIISRRKSKDLILKYVFGATIIAFISLLPIYLQGGLVAMTVEVIIAPLYAGETQSFLYRLVKGVTHLKLMIPIALLGMAGILLGFLDDIRERWWVVGLLLWFCIQIFILDYDGADDLFLGIILVSMGIGFAFEKLSTKYESERINSIVTAVVVCMLIWQVVTLGGVGVITNPYSYSGDGPDQAILESGIQQFAHLSGYTEYTIGGSPPDEQYNVKSRYGPDKIEELFFTSTIPSTCHYRLSGMELEWMNLTEQSFTEEKCGKWRLP
Protein: Probable RNA polymerase II nuclear localization protein SLC7A6OS (Solute carrier family 7 member 6 opposite strand transcript homolog) (Q7TPE5)
Organism: Mus musculus (Mouse)
Function: Directs RNA polymerase II nuclear import.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerase II subunit RPB2
- DNA-directed RNA polymerase II subunit RPB9
- DNA-directed RNA polymerase II subunit RPB4
Sequence:
MEAGRTAVLRVKRKRNAEPAEALVLACKRPRSSEVESAARETPEGQEAAAAERNVFQLVATVRSQEEPIQQLVRAALRPSRSSQLRIRRDLRASVREVRKEGRYRVVSSHRSSGTSNSLEPQCGSEAVGDAGFQLLDLVHEEENPEAAATDCRKTSDPDVILCNSVELIRERLTVSEDGSQVNHQEDPKHNDDYVYDIYYMEMAPPGWIENIMSVQPYSQEWELVNDDEQSEDIYEDEDDENSENNWRNEYPDEESSDRDEDSRGSDEYNSLSEEERSCERLMWSKYPLDVQKEFDYDSPHGLDSD
Protein: Intelectin-1 (Embryonic epidermal lectin) (Xeel) (Q5PPM0)
Organism: Xenopus laevis (African clawed frog)
Function: Lectin that specifically recognizes microbial carbohydrate chains in a calcium-dependent manner. Binds to microbial glycans that contain a terminal acyclic 1,2-diol moiety, including beta-linked D-galactofuranose (beta-Galf) and D-phosphoglycerol-modified glycans. Binds to S.pneumoniae serotypes with glycans that contain beta-linked D-galactofuranose (beta-Galf) and with D-phosphoglycerol-modified glycans. Can bind a variety of monosaccharides (in vitro). Probably plays a role in the defense system against microorganisms (Probable).
Subcellular location: Secreted {ECO:0000269|PubMed:15537792, ECO:0000305|PubMed:26755729}. Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:15537792}.
Interaction partners:
Sequence:
MLSYSLLLLALAFPAGHAGSCEQASISEKKEKILNLLACWTEGNADNSLSRSGGSPTGDMNYGYRSCNEIKSSDSRAPDGIYTLATEDGESYQTFCDMTTNGGGWTLVASVHENNMFGKCTVGDRWSTQQGNMLQNPEGDGNWANYATFGLPEGATSDDYKNPGYYDIEAKNLALWHVPNKTPMVMWRNSSILRYRTQNGFLTEEGGNLFELYKKYPVKYDIGKCLADNGPAVPVVYDLGSAEKTASLYSPNGRSEFTPGFVQFRAVNSERATLALCAGVKVKGCNVEHHCIGGGGYIPEGSPRQCGDFAALDWDGYGTNLGWSASKQIIEAAVMLFYR
Protein: L-cysteine S-thiosulfotransferase subunit SoxA (EC 2.8.5.2) (Cytochrome c551 subunit diheme) (Protein SoxA) (SoxAX cytochrome complex subunit A) (Sulfur oxidizing protein A) (Thiosulfate-oxidizing multienzyme system protein SoxA) (TOMES protein SoxA) (Q9K4M4)
Organism: Pseudaminobacter salicylatoxidans
Function: C-type diheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosulfate or other inorganic sulfur substrates. This leads to the liberation of two electrons, which may be transferred from the SoxAX complex to another cytochrome c that then channels them into the respiratory electron transport chain. Some electrons may be used for reductive CO(2) fixation.
Subcellular location: Periplasm {ECO:0000250|UniProtKB:Q939U1}.
Interaction partners:
- Monoheme cytochrome SoxX
- Sulfur compound chelating protein SoxZ
- Thiosulfate-binding protein SoxY
- Sulfur dehydrogenase subunit SoxC
- Cytochrome c
- Sulfate thiol esterase SoxB
- Cbb3-type cytochrome c oxidase subunit
- Cytochrome c oxidase subunit 2
- Thioredoxin-related protein
- DMSO/TMAO reductase YedYZ molybdopterin-dependent catalytic subunit
Sequence:
MTVSKRFLAPVFAMVGGLVLAFSANADPVDEELVIDDIPMVTRAAAPEGHPFDEGLSGWLFREAETRETEADSFANPGMLAVERGADIWNTVEGSAGKSCASCHDDAATSMKNVGAQYPKWDADAKRPINIELQIDKCRVENMGAEPYKFDAEGQVALTSYIKHQSLGTPVKMDLSDGELQDWWEKGKELYYTRTGQLNFACASCHEDSMGKYIRADHLSQGQANGFPTYRFNTGGMVSLHNRFRGCIRDTRAEMPKAFSDELMALEVYVTWRGTGLSVETPAVRQ
Protein: Glutathione S-transferase (EC 2.5.1.18) (X5DR03)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPMILGYWDIRGLAHAIRLLLEYTDSSYEEKKYTMGDAPDYDRSQWLNEKFKLGLDFPNLPYLIDGAHKITQSNAILCYIARKHNLCGETEEEKIRVDILENQTMDNHMQLGMICYNPEFEKLKPKYLEELPEKLKLYSEFLGKRPWFAGNKITFVDFLVYDVLDLHRIFEPKCLDAFPNLKDFISRFEGLEKISAYMKSSRFLPRPVFSKMAVWGNK
Protein: Ribonuclease VapC22 (RNase VapC22) (EC 3.1.-.-) (Toxin VapC22) (P71623)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Toxic component of a type II toxin-antitoxin (TA) system. An RNase (By similarity). Upon expression in M.smegmatis inhibits translation and colony formation. Its toxic effect on colony formation is neutralized by coexpression with cognate antitoxin VapB22; the effect on translation has not been tested but is probably neutralized also.
Subcellular location: Secreted. Note=Following 6 weeks of nutrient starvation. {ECO:0000269|PubMed:23345537}.
Interaction partners:
- Antitoxin VapB22
- Probable enoyl-CoA hydratase EchA16
- DUF2277 domain-containing protein
- DUF1802 family protein
Sequence:
MTTVLLDSHVAYWWSAEPQRLSMAASQAIEHADELAVAAISWFELAWLAEQERIQLAIPVLSWLQQLAEHVRTVGITPSVAATAVALPSSFPGDPADRLIYATAIEHGWRLVTKDRRLRSHRHPRPVTVW
Protein: Ciliary microtubule inner protein 2B (Q2TBR5)
Organism: Bos taurus (Bovine)
Function: Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:34715025}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:A2AIP0}.
Interaction partners:
- Tektin-4
- Meiosis-specific nuclear structural protein 1
- Tektin-3
- Outer dynein arm-docking complex subunit 2
- Cilia- and flagella-associated protein 276
- Tektin-1
- Outer dynein arm-docking complex subunit 3
- Tektin-2
- Outer dynein arm-docking complex subunit 4
- Cilia and flagella associated protein 45.
Sequence:
MASTFIPGLNPQNPHYIPGYTGHCPLLRFSMGQTYGQMTGQLLRGSPGLAWPPAHRTLLPPIQPPRSPEPRRRSLPVRPGHERLSSSMVPGYTGFVPQAQFIFAKNCSQVWAEALNGFTQRNGGQGSQELPKEAKGEKDVEKDQEPKPEVEKEPELGQEAEQASPYSMDDRDPRKFFMSGFTGYVPRARFLFGSSFPVLSNQALQEFGEMKSPGRSQKDPKHLPALSRTYPQHLGLLPKYGGYVPGYKFQFGRTYGHLTQDALGLSTLQKQLLV
Protein: Visgun, isoform E (M9PHX2)
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:
MNRQAKFLILCLFVGLFSANLCEEVTTPAPADTTTQESKNTTTPPDTTTTVTPPSTSTTSTTTEKTTTTPPITTSTEKTTTSTTPASTTSSTTPASTTSSTTPATTTTTPGTTSTTTPSPNSTTTTPPPHTSTTPAPKPVPCGHFDGSSFIGGIVLTLGLLAIGLVAYKFYKARNERNYHTLXAATAFTSAFNAAAGAAAASSSAASTDAERVRFVQPSIPLRSPPTQPPPPPPTHMGGSGGGAAAAPQNCSPSARDRLLHT
Protein: Guanine nucleotide-binding protein alpha-17 subunit (Odorant response abnormal protein 3) (Q18434)
Organism: Caenorhabditis elegans
Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. This specific G-alpha subunit plays an important role in olfaction and in cilia morphogenesis. Involved in chemotactic responses to attractants diacetyl, pyrazine, 2,4,5-trimethylthiazole, benzaldehyde, isoamyl alcohol, butanone and 2,3-pentanedione. Displays a redundant function with gpa-3 in chemotactic responses. Plays a role in the avoidance response to the noxious chemical quinine in ASH sensory neurons. Involved in avoidance responses to copper, sodium dodecyl sulfate and linoleic acid. Involved in osmotic avoidance and mechanosensory responses. Involved in specifying fan-like morphology of cilia of head sensory neurons AWC. Plays a role in the detection of preferred food sources by mediating the recognition of food odors in olfactory sensory neurons.
Subcellular location: Cell projection, cilium {ECO:0000269|PubMed:15342507}. Cell projection, dendrite {ECO:0000269|PubMed:15342507}. Note=In amphid neurons also weakly expressed in cell body. In phasmid neurons found only in cilia.
Interaction partners:
- Receptor-type guanylate cyclase gcy-10
- Guanine nucleotide-binding protein subunit gamma
- Cyclic nucleotide-binding domain-containing protein
- Cyclic nucleotide-gated channel
- Receptor-type guanylate cyclase daf-11
- Guanine nucleotide-binding protein subunit beta-2
- Guanine nucleotide-binding protein subunit beta-1
- Ion transport domain-containing protein
- Ion transport domain-containing protein
- Serpentine receptor class r-10
Sequence:
MGSCQSNENSEGNARNKEIEKQLNADKRAGSSIVKLLLLGAGECGKSTVLKQMQILHSNGFTEEEVNEKRAIVYNNTVSAMCTILRAMDGVLHLPLENGQKEAEKAIVMKVQENGEEGEALTEEVSKAIQSLWADPGVKKAFEMRSEYQLPDSAKYFLDNCQRISEPGYRPNDQDILYSRVATTGVVEVKFKIKELDFRVFDVGGQRSERRKWIHCFDNVESIIFITAISEYDQVLFEDETTNRMIESMQLFNSICNSTWFLSTAMILFMNKKDLFMEKIQRVNITTAFPDYEGGQNYEEAVSFIKQKFAELNLNPDKKTIYMHETCATDTNQVQLVISSVIDTIIQKNLQKAGMM
Protein: Hydroxyacyl-thioester dehydratase type 2, mitochondrial (EC 4.2.1.-) (3-hydroxyacyl-[acyl-carrier-protein] dehydratase) (P38790)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mitochondrial 3-hydroxyacyl-thioester dehydratase involved in fatty acid biosynthesis. Required for respiratory growth and for normal mitochondrial morphology.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15387819, ECO:0000269|PubMed:16823961}.
Interaction partners:
- 3-oxoacyl-[acyl-carrier-protein] reductase
- Enoyl-[acyl-carrier-protein] reductase, mitochondrial
- Fatty acid synthase subunit alpha reductase
- Fatty acid synthase subunit beta dehydratase; Enoyl-[acyl-carrier-protein] reductase; [Acyl-carrier-protein] acetyltransferase; [Acyl-carrier-protein] malonyltransferase; S-acyl fatty acid synthase thioesterase]
- 3-oxoacyl-[acyl-carrier-protein] synthase homolog
- Peroxisomal hydratase-dehydrogenase-epimerase
- Putative lipoate-protein ligase A
- Malonyl CoA-acyl carrier protein transacylase, mitochondrial
- Acetolactate synthase catalytic subunit, mitochondrial
- 2-hydroxyacyl-CoA lyase
Sequence:
MKSKTWIFRDVLSSHRTKAFDSLLCRRLPVSKATKHLQLGEHFLFFPPSFEKLDRDGYFNYQNPASLLGNPDLRYRRRIWGQGELVQYLPVTLDQEYTCHESIKYVKKIRDEHVVCIERTLLQERPENVSSPMDICLFERRVLMYTNSPANKTAVKMPVGEENYKILKNFTVTDMDIVAYGQMSLNPHRIHWDKEYSRYVEGYDDIIMQGPFSVQLLQKCIQPFLEQPIRQLRYRNLNYIYPNTTLSICQSLSSSSGMYTFQIRDLQKANLVYMKADVFC
Protein: ADM5 [Cleaved into: Adrenomedullin-5 (AM5)] (A5LHG2)
Organism: Sus scrofa (Pig)
Function: Seems to have a peripheral vasodepressor effect and a central vasopressor effect.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MTAHILLLWLFASSILGDPDSAGRLTRHQVSLKSGRLCSLGTCQTHRLPEIIYWLRSASTKELSGKAGRKPQDPYSYGRRRRRRRRRREARLLRRLQDPSLRRAQLAG
Protein: BAG cochaperone 1 (C9JYK5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNRSQEVTRDEESTRSEEVTREEMAAAGLTVTVTHSECRAPGNEKHDLHVTSQQGSSEPVVQDLAQVVEEVIGVPQSFQKLIFKGKSLKEMETPLSALGIQDGCRVMLIGKKNSPQEEVELKKLKHLEKSVEKIADQLEELNKELTGIQQ
Protein: Flotillin-2 (Reggie-1) (REG-1) (Q9Z2S9)
Organism: Rattus norvegicus (Rat)
Function: May play a role in axon growth and regeneration. May be involved in epidermal cell adhesion and epidermal structure and function.
Subcellular location: Membrane {ECO:0000269|PubMed:9858255}. Endosome {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:Q14254}; Lipid-anchor {ECO:0000250|UniProtKB:Q14254}. Note=In neuronal cells, associated with GPI-anchored cell-adhesion molecules.
Interaction partners:
- Flotillin-1
- Caveolin-1
- Cadherin-1
- E3 ubiquitin-protein ligase CBL
- Sorbin and SH3 domain-containing protein 1
- Stomatin
- Catenin beta-1
- Catenin alpha-1
- Sodium-dependent dopamine transporter
- Coronin
Sequence:
MGNCHTVGPNEALVVSGGCCGSDYKQYVFGGWAWAWWCISDTQRISLEIMTLQPRCEDVETAEGVALTVTGVAQVKIMTEKELLAVACEQFLGKNVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSSLGKTQTAVVQRDADIGVAEAERDAGIREAECKKEMLDVKFMADTKIADSKRAFELQKSAFSEEVNIKTAEAQLAYELQGAREQQKIRQEEIEIEVVQRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEAAVIEAMGKAEAERMKLKAEAYQKYGDAAKMALVLEALPQIAAKISAPLTKVDEIVVLSGDNSKVTSEVNRLLAELPASVHALTGVDLSKIPLIKNATGAQV
Protein: Integrase-type DNA-binding superfamily protein (F4JS76)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MRIHEKGGGGRRKVKHSEVDMVSLRRRRLLGLCCGPNGYVTPLPFLTAEEMITGIPNPNARAAYNPGPAETVTTVIVEKKAIEERSRRTRSKHMHFRSDYSDISPVNSDSISPKYQPPKRRKQHRRKRVHNQEPCLMRGVYYKNMKWQAAIKVEKKQIHLGTFSSQEEAARLYDRAAFMCGREPNFELSEEVIRELKQQSWEEFLNCTRRTITNKKPKSRIEHEDTKINASMPHQPEEEEQDSDKM
Protein: Peptidyl-prolyl cis-trans isomerase-like 3 (PPIase) (EC 5.2.1.8) (Cyclophilin J) (CyPJ) (Cyclophilin-like protein PPIL3) (Rotamase PPIL3) (Q9H2H8)
Organism: Homo sapiens (Human)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be involved in pre-mRNA splicing.
Interaction partners:
- Pre-mRNA-splicing factor SLU7
- Peptidyl-prolyl cis-trans isomerase-like 1
- Pre-mRNA-splicing factor SYF2
- Pre-mRNA-processing factor 17
- Spliceosome-associated protein CWC27 homolog
- E3 ubiquitin-protein ligase RNF113A
- Eukaryotic initiation factor 4A-III
- Coiled-coil domain-containing protein 12
- Spliceosome RNA helicase DDX39B
- Pre-mRNA-splicing factor CWC22 homolog
Sequence:
MSVTLHTDVGDIKIEVFCERTPKTCENFLALCASNYYNGCIFHRNIKGFMVQTGDPTGTGRGGNSIWGKKFEDEYSEYLKHNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVNEKTYRPLNDVHIKDITIHANPFAQ
Protein: Homeobox protein SIX6 (Homeodomain protein OPTX2) (Optic homeobox 2) (Sine oculis homeobox homolog 6) (O95475)
Organism: Homo sapiens (Human)
Function: May be involved in eye development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
- Homeobox protein OTX2
- Dachshund homolog 1
- TLE family member 5
- Transducin-like enhancer protein 1
- Visual system homeobox 2
- Protein phosphatase EYA2
- Calcium load-activated calcium channel
- Protein phosphatase EYA1
Sequence:
MFQLPILNFSPQQVAGVCETLEESGDVERLGRFLWSLPVAPAACEALNKNESVLRARAIVAFHGGNYRELYHILENHKFTKESHAKLQALWLEAHYQEAEKLRGRPLGPVDKYRVRKKFPLPRTIWDGEQKTHCFKERTRHLLREWYLQDPYPNPSKKRELAQATGLTPTQVGNWFKNRRQRDRAAAAKNRLQQQVLSQGSGRALRAEGDGTPEVLGVATSPAASLSSKAATSAISITSSDSECDI
Protein: Microsomal triglyceride transfer protein homolog (Defecation suppressor of clk-1) (G5ECG7)
Organism: Caenorhabditis elegans
Function: Catalyzes the transport of cholesteryl ester, and phospholipid between phospholipid surfaces (By similarity). Does not catalyze transport of triglycerides. Required for the assembly and secretion of plasma lipoproteins that contain apolipoprotein B. Required for normal expression of klf-3.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:17924655}.
Interaction partners:
- Protein disulfide-isomerase 2
- Phospholipid/glycerol acyltransferase domain-containing protein
- Vitellogenin-6
- Vitellogenin-1
- Vitellogenin-5
- Sterol regulatory element binding protein sbp-1
- Vitellogenin-2
- 3-hydroxy-3-methylglutaryl coenzyme A reductase
- Vitellogenin-3
- Vitellogenin-4
Sequence:
MFSSRIWLLLAVTVGVCLAVPDLDEIKKNLRKHGPDYYKNQPKMNENTVRLLKVDYWFRTESMIYDDIDNKEKDPSTVIAGNFSFETLHHDVEGGMLGRFTLTQCNTDNCGNPSPIYIAFRQGGNNAEHILKASDESDATWNFLYAIVNTIYTPAEYGEGDEQTVDTIYGRCFVNFGRPEDKRFRRIIEKCDLGYGTNFTKFEGIESVQYDQDVWYTQNTKVDADIIMVDAIEMLAFKSPLHEKYGFTLESRTHVEITNRTRVFVTSYCNDTVPSAKCAEQAFGAVRVGGKLYEHVKIAQEQSNKLTKLIGTYRRHLQDMGDSHICEKHSLLYSQIAQEARLAKRQDWEAAIQYPENDHVLSLIASALGGVGTAESITTAREVLLTASPDYLDDLLFGISQSSSNNEKWHKQLMYWLGSLDKKSEEYWKVANTIATVLNKRCEASTSSLNSCNKGKETIVNKFITDLTAGGVEVRVLEVLENIPIFGSYTFAKKFICETESEDVQKAALNVILAASKNLYETQLTHKLIKLFRNTCSQETPTSHSQLAIDILLKCVPDHQNVATLILRTETLNPDDQEKWHYLYKAIEASGNKDELKAEFWSRMRKFKVFRPNFLHRALQADSHVHWQEIADASNFQLFSTANTEFLQKSFKRSIFELSMKKGRKEHNLFSLSIDTEHLEQFVTGSASSRSGAPQGSVRIGVAGHKLPTHHIFKGSTDLLSTVWEADGRTHKAFEGHVPVRDVRLSVPLLSGLTLDVDSVGAISMRVLASAEVSLWNQRSNAKAEAYTSGSLHLTASLYHHSEPVRHVESTISALSTFTTDTRAIFETLPYDFCLRTSNSNVDINQKTVVQDQIGKHKKKTLNRKRVHPGVTYRLDDSTIRQCNSYLEQFRL
Protein: SH3-containing GRB2-like protein 3-interacting protein 1 (Endophilin-3-interacting protein) (Q6IZA3)
Organism: Psammomys obesus (Fat sand rat)
Function: May function in clathrin-mediated endocytosis. Has both a membrane binding/tubulating activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. Has a preference for membranes enriched in phosphatidylserine and phosphoinositides and is required for the endocytosis of the transferrin receptor. May also bind tubulin. May play a role in the regulation of energy homeostasis.
Subcellular location: Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:Q9BQI5}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9BQI5}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9BQI5}.
Interaction partners:
Sequence:
MMEGLKKRTRKAFGIRKKEKDTDSTGSPDRDGMQPSPHELPYHSKAECAREGGNKASKKSNGAPNGFYAEIDWERYNSPELDEEGYSIRPEEPGSTKGKHFYSSSESEEEEESHKKFNIKIKPLQSKDILKNAATVDELKASIGNIALSPSPVRKSPRRSPGAIKRNLSSEEVARPRRSTPTPELTSKKPLDDTLALAPLFGPPLESAFDGHKTEVLLDQPEIWGSGQPVNPSMESPKLARPFPTGTPPPLPPKTVPATPPRTGSPLTVATGNDQAATEAKIEKLPSISDLDSIFGPVLSPKSVAVNTEETWVHFSDASPEHVTPELTPREKVVTPPAASDIPADSPTPGPPGPPGSAGPPGPPGPRNVPSPLNLEEVQKKVAEQTFIKDDYLETLSSPKECGLGQRATPPPPPPPTYRTVVSSPGPGSGSGTGTASGASSPARPATPLVPCSCSTPPPPPPRPPSRPKLPPGKPGVGDVSRPFSPPIHSSSPPPIAPLARAESTSSISSTNSLSAATTPTVENEQXSLVWFDRGKFYLTFEGSSRGPSPLTMGAQDTLPVAAAFTETVNAYFKGADPSKCIVKITGEMVLSFPAGITRHFANNPSPAALTFRVINSSRLEHVLPNPQLLCCDNTQNDANTKEFWVNMPNLMTHLKKVSEQKPQATYYNVDMLKYQVSAQGIQSTPLNLAVNWRCEPSSTDLRIDYKYNTDAMSTAVALNNVQFLVPIDGGVTKLQAVLPPAVWNAEQQRILWKIPDISQKSENGGVGSLLARFQLAEGPSKPSPLVVQFTSEGSTLSGCDIELVGAGYGFSLIKKRFAAGKYLADN