wanglab/gogpt-training-data huggingface dataset:
Protein: mRNA-binding protein PUF1 (Q8I3S3)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- CCR4-associated factor 1
Sequence:
MYICLYNIFYFICSKMENTKRKENDNCKEYALNISSKTNKEKYKYEGKKKDEKKKKDEGEYTNDDNKYVNDENKYVNDDNKYVNDENKYVNDENKYVNNDNKYVNNDNKYVNNDNKYTYDENTKKDKVDINIDIYNDDNQSYNNKKQKNDDDDISHNKHKNGDDKIDNIDNIDNNIEKGDNNICNFYDKRNEDNNTYADCNNIVEGINNNFECSGKKCNYIDKQRDKTKKYDIINMKCDNKCSNNMKNSTKNKMNTQTNNNKDMLSNQIRMCSKNINNNYIYNNNNNNNSIISSNYYYNYYNNTNMYNELNMVHNEKNNLIDILDKELKKNCNNYNIGNNNMNCNYKPNYNYFINKDLLNNNMTYIYNYPMMNTLNYSKDNNYCTYLDEINRINECTYNTTQPNLNNNTTYSPNFNDNSNLLYNHESYILSPYDYYNYYCSGLIPTYPIFNYRNVINSNNNNNNINGNINNNINGNINNNINGNINNNMNGNINNNMNGNINNNIHSNINNNSNNNNSNNNSNNNNKHYYDNTYFNHIIPSNTNNNSIDTYNENNNNHKMFYNYNKYNMYAPKIYYHDNMHNLYPINNIPSNYNSTENKILNCNTIIPYTGTNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNILSKNIVPYNANDINNLINLNNDNINNNSHMNPNNNTQIFNYFNYVSNSNFNIQRYLSNNNNNNNNLNNSTDYQQNISYYNTYNSNCYSSASKTYYCNQYLNEYPLFPVSSIDLYNTDNMNYTSNQLYYYHGNDNMNNEELKKKAEQENTHNNVNMNKRGVQNKKNNYNKENYLSPISFTGNICKIAKDQTGCRILQRILEKKNPKHIEEIYNEALDHIIELMVDPFGNYLCQKLMEVCTSEQIEKIIDKSSDQLINASISVHGTRTVQKLIEMIKTPSQIKKTTKALKNSIITLIKDINGNHVVQKCLITLTSHQCDFIYEAILNNCVEVSTHRHGCCVIQRCIDSANEAQKELFIRNISNNALDLVQDAFGNYVVQYILNLGNEKVNLEIANKLLPNIEELAVQKFSSNVVEKCLIIGNNKCRKLIINEILKKDKDILKQIILDPFGNYVIQRALSVASEPELTKLVEGIKPYIKELRNISSGKRIAWKLAKKHPLLNADINNQYFSNDNSDNVSLQNHDISSTNNSINIPTNNSDIFKNDKKKNNDENIVKKNYNNNNNNNNNNVKTFNHSKNYNAKNFNNNPNGNIKNFTNDNMKSYNYEHMRNYNFDPIRNYNMDNMKNYNVDNMKNYNVDNMKNYNMDNMKNYNMDNMKNFNNEYVKNFNNEYVKNYNNEYVKNYNNEYVKNYNNEYVKNYHHNNIKNHINCSNNSYANNSKTYKKNTQQKKNLQSSNDLCNVVSYNDHSPQNIAHKKNNLQEKISNVYNKRNDDSSMNNNTFCYKQGYVPDDTMKTHNETKNNDKMDEMDNLTTNEREHLNKIYSNQEDNQNKKDDIYHTHKRNDESNIYENQRNFNKNNFKYVIGQNLHRDDNNILVCNKSKTDRENNVRININEKNEEKNVDGQEKNENIQEKIDNVQEKKDNIQEKNENIQEKKDNVQEKNENIQEKKDNVQEKNENIQEKKDNVQEKNENIQEKNENIQEKNENIQEKNENIQRKKNNVQGKNENSQEKQENIQVKKEYVNEKKECIDDEEQKEPFHNNANTQNDNKCNNNVIKKSSVHLDNEKYHYENNINTEKEHIRSKSNHNRINNNSYDNKMIEKQNNENSNKYIIQNVPNNNSRMFHKKNDENKDGTKNKHMENKNNKVYNNNFNKNEYKRIQNNQMNMNQSYNFSQNKNYVYNNSYNNYNENYVNFYPMRNNNQDFNSNICSSNKNNPKLTYISNNKNNGDNYMRKNPKKITKKYSNESKLI
Protein: Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 3 (EC 2.4.1.102) (EC 2.4.1.148) (EC 2.4.1.150) (C2GnT-mucin type) (C2GnT-M) (dI/C2/C4GnT) (dIGnT) (Q8CH87)
Organism: Rattus norvegicus (Rat)
Function: Glycosyltransferase that can synthesize all known mucin beta 6 N-acetylglucosaminides. Mediates core 2 and core 4 O-glycan branching, 2 important steps in mucin-type biosynthesis. Has also I-branching enzyme activity by converting linear into branched poly-N-acetyllactosaminoglycans, leading to introduce the blood group I antigen during embryonic development.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- C1GALT1-specific chaperone 1
- Hexosyltransferase
- ST3 beta-galactoside alpha-2,3-sialyltransferase 1
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2
- Glucosaminyl
- Glucosaminyl
Sequence:
MVSWRRFCWHYHGWTLGCYMLLAIIALKLSLRLKCDFDVMDLDSKEFQSQYCRDLLYKTLELPAKSSINCSGVIRGEQKAVTQALLNNLELKRKRQSFTEADYLSMTADCEHFKTQRKFIQVPLSKEEANFPIAYSMVIHEKIENFERLLRAVYTPQNIYCVHVDQKSSETFQQAVRAIVSCFPNVFIANKLVSVVYASWSRVQADLNCMEDLLQSPVPWEYLLNTCGTDFPIKTNAEMVKALKLLNGQNSMESEVPPPHKTFRWKYHYEVADTLYRTSKEKTPPPNNITMFTGNAYMVASRDFIEHVLSNSKARQLIEWVKDTYSPDEHLWATLQRASWMPGSDPLHPKFDLSDMRSIARLTKWQDHEGDIENGAPYTSCSGIHQRAICVYGSGDLHWILQNHHLLANKFDPKVDDNVLQCLEEYLRHKAIYGTEL
Protein: Retinol dehydrogenase 13 (EC 1.1.1.300) (Q8CEE7)
Organism: Mus musculus (Mouse)
Function: Retinol dehydrogenase with a clear preference for NADP. Oxidizes all-trans-retinol, but seems to reduce all-trans-retinal with much higher efficiency. Has no activity towards steroid.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q8NBN7}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8NBN7}. Note=Localized on the outer side of the inner mitochondrial membrane. {ECO:0000250|UniProtKB:Q8NBN7}.
Interaction partners:
Sequence:
MSRFLLPVSVVGTVIGGTVLLKDYVAGGACPSKATIPGKTVIVTGANTGIGKQTALELAKRGGNVILACRDMEKCEVAAKDIRGETLNPRVRAERLDLASLKSIREFARKVIKEEERVDILVNNAAVMRCPHWTTEDGFEMQFGVNYLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDFEDLNWQMKKYDTKAAYCQSKLAVVLFTKELSHRLQGSGVTVNALHPGVARTELGRHTGMHNSAFSGFMLGPFFWLLFKSPQLAAQPSTYLAVAEELENVSGKYFDGLREKAPSPEAEDEEVARRLWTESARLVGLAMAHGSPGRGHAIPR
Protein: Putative carnobacteriocin-B2 immunity protein (Carnocin-CP52 immunity protein) (P38582)
Organism: Carnobacterium maltaromaticum (Carnobacterium piscicola)
Function: Could impart immunity to carnobacteriocin-B2 to naturally sensitive host strains.
Interaction partners:
Sequence:
MDIKSQTLYLNLSEAYKDPEVKANEFLSKLVVQCAGKLTASNSENSYIEVISLLSRGISSYYLSHKRIIPSSMLTIYTQIQKDIKNGNIDTEKLRKYEIAKGLMSVPYIYF
Protein: Protein bicaudal D homolog (V6CJ04)
Organism: Caenorhabditis elegans
Function: Part of a complex with dlc-1 and egal-1, which is recruited to the nuclear envelope by unc-83, where in turn, it recruits dynein to the nuclear surface and regulates nuclear migration in hypodermal precursor cells (Probable). Required for the formation of dendritic branches of PVD sensory neurons.
Subcellular location: Nucleus envelope {ECO:0000305|PubMed:20005871}. Perikaryon {ECO:0000269|PubMed:21205795}. Cell projection, dendrite {ECO:0000269|PubMed:21205795}. Note=Probably recruited to the nuclear envelope by unc-83. {ECO:0000305|PubMed:20005871}.
Interaction partners:
- Egalitarian protein homolog
- Dynactin subunit 1
- Probable dynactin subunit 2
- Dynein light intermediate chain
- Dynein heavy chain, cytoplasmic
- WD_REPEATS_REGION domain-containing protein
- Protein nud-2
- Ras-related protein rab-6.1
- Ras-related protein rab-6.2
- Nuclear migration protein unc-83
Sequence:
MAESELEKLRQDIAILTEKYEQAKEDIHKAANAGLELLRQKEDLEKRLAEMQAELDLARTEIDKTNQTLAEYRSQHQRSTRSELENEESLLEESSAKEEEYLQRIAKLEADLKKKEQELAEKKEELESIEKKHSKEIDSGAALEDERRKLRAELKETKEREQRLISEYSELEEENIGLQKTVANLRGSQVEYESLRIDNNRLEETIEIMKMAAEEDEILRVIADKQLEEALLTAQQERDQRLAMKRELEQTRNAEHISSLNDMLFGLERLGEDGELPPPQPGASDLFSELQGSSDVKVRELEAAKEGLQEELKSREKIFIEFVTGLADTLNIHRPTNELDYMHARQQKDVVLEKIQNIARDTDRHDKEGEEKRSGILKADLRTLVLVAGEKSAQLAAAQDAMIQVSDQLYQFYHQMTQNQGVQTEKSVQEIVKKLRLLARANAEDVPRVSLADEGVESGTETDVNASRSIPLNSDRLVIAPSFAKEIEKKLASVKIGDVLSETDLRQRILTEGNAISETTESLKKMIQVVKRTSEQAFNQAVMASGAENEIEMQNMKLRSLLSTKRDQISTLRTVLKSNKLTAESALTSMREKYESEKKMMMEINDKMRRELKQLKEDAATFASHRAMFTARGEELKSKVEELSNELRANEEEKKTLNQLLRLAIQQKLTLTQRLEEVEVDRDRQVFKRSSTRAPTRETYQPPRAVRYPGSTTTAQQPAPSSSGGSRGGPRRGDNQQ
Protein: Tubulin polyglutamylase complex subunit 1 (PGs1) (Q6ZTW0)
Organism: Homo sapiens (Human)
Function: Subunit of the tubulin polyglutamylase complex (TPGC). The complex mediates cilia and flagella polyglutamylation which is essential for their biogenesis and motility (Probable). May act in the targeting of the tubulin polyglutamylase complex. Required for the development of the spermatid flagellum (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q99MS8}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q99MS8}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q99MS8}. Cytoplasm, cytoskeleton, flagellum basal body {ECO:0000250|UniProtKB:Q99MS8}. Cell projection, axon {ECO:0000250|UniProtKB:Q99MS8}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q99MS8}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q99MS8}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000269|PubMed:34782749}. Note=Associated with microtubules from neurites, centrosomes, basal bodies and axonemes. {ECO:0000250|UniProtKB:Q99MS8}.
Interaction partners:
- Leucine-rich repeat-containing protein 49
- Nicolin-1
- Polyglutamylase complex subunit TTLL1
- Tubulin polyglutamylase complex subunit 2
- Centriolar satellite-associated tubulin polyglutamylase complex regulator 1
Sequence:
MAAVEKRRQAVPPPAGFTDSGRQSVSRAAGAAESEEDFLRQVGVTEMLRAALLKVLEARPEEPIAFLAHYFENMGLRSPVNGGAGEPPGQLLLQQQRLGRALWHLRLAHHSQRAAFNNNVSVAYECLSAGGRRKRPGLDGRTYSELLRRICRDGQAPEEVVAPLLRKVQCRDHEAVPLSVFRAGTLTCFVLLEFVARAGALFQLLEDSAAAVADRRVGQAVLDTLEGALQASDAAAPARFLEAGSRLGPDSLALALDRAVGGRRPSAPMTREEFLERAAALFIAKVKPVG
Protein: Transcription elongation factor SPT4 (DRB sensitivity-inducing factor small subunit) (DSIF small subunit) (dSpt4) (Q9TVQ5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the DRB sensitivity-inducing factor complex (DSIF complex), which regulates transcription elongation by RNA polymerase II. DSIF enhances transcriptional pausing at sites proximal to the promoter, which may facilitate the assembly of an elongation competent RNA polymerase II complex. DSIF may also promote transcriptional elongation within coding regions. DSIF is required for the transcriptional induction of heat shock response genes and regulation of genes which control anterior-posterior patterning during embryonic development (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- DNA-directed RNA polymerase II subunit RPB3
- Transcription elongation factor SPT5
- Transcription elongation factor SPT6
- FACT complex subunit spt16
- DNA-directed RNA polymerase II subunit RPB1
- FACT complex subunit Ssrp1
- DNA-directed RNA polymerase II subunit RPB7
- DNA-directed RNA polymerase II subunit RPB2
- DNA-directed RNA polymerase II subunit RPB11
- RNA polymerase II-associated factor 1 homolog
Sequence:
MAFDAIPKDLRGLRACLVCSLVKSFDQFETDGCENCEEFLRMKNNKDNVYDHTSNNFDGIIALTTPTDSWVAKWQRLSRFTRGIYAISVSGTLPQSTLRDMKNRGIVYKSRDRSQR
Protein: Uncharacterized protein RP027 (Q9ZEB7)
Organism: Rickettsia prowazekii (strain Madrid E)
Interaction partners:
- Uncharacterized protein RP028
- Outer membrane protein B
Sequence:
MDFITNRKFRSTLLCHQNIPINRKIEFENLKDFYTTFNIRPISSENKIDLNNEQENISFYYENLPEPFISTTSAIMKAILYVYAENISNPIRLEQVAKEAFKKLGKYQLQDFLAILEQHFITFIFQGYLKIFETKPHAIATITEKPKTSQFVRYQAKHAHFNNVTNMLSVTNRLNDMIGIPIHEKYILEMLDGTHNIDDIKKGMIEKINSKLLIACDNKGQAVTDPKLLKEFVDYIVNISLEKFRINYLLIG
Protein: LRR47 (Q24386)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKILCEVQVVNRATQTNKTPRPVKSTLAIGYKQSARDANGNTKKELEMVLFSGQNKTGNRYKVKDNIHVVHTKFVLDGKTTIGFIQPPDNLLIKCDPIQLKGFLQTLKLGMDGKDAINLRLNINAATAIPQKAQPQVRMVISKRSEYPIKGFPRTLKSLTINNSQLVKLSFEICTLRNLTKLDVSGNKLAKIPSELGRLPLTSLHLGNNLLGTQNDWCWLRGTKLCQSLGELDLSGNGLTYFPPPLVKFESLVSLNLNNNLLSRLPFAIRRMKALRKLYVCSNELESLPSAVEDLRIDLLDVWGNCFKEFNADAAQKMCLQKAASNSPQPLWLLGARAVDKYMLPLSAGSIPAVLIDLIREAPRCPCGELCYAQRKEDLFQRVVQPKFISVKNLTYSREHQIYADVVLCDSRCSASAELKLLFNIIFS
Protein: Thioredoxin-dependent peroxide reductase, mitochondrial (EC 1.11.1.24) (Antioxidant protein 1) (AOP-1) (PRX III) (Perioredoxin-3) (Protein MER5) (Thioredoxin-dependent peroxiredoxin 3) (P20108)
Organism: Mus musculus (Mouse)
Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. Acts synergistically with MAP3K13 to regulate the activation of NF-kappa-B in the cytosol (By similarity). Required for the maintenance of physical strength.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:9497357}. Cytoplasm {ECO:0000250|UniProtKB:P30048}. Early endosome {ECO:0000250|UniProtKB:P30048}. Note=Localizes to early endosomes in a RPS6KC1-dependent manner. {ECO:0000250|UniProtKB:P30048}.
Interaction partners:
- Peroxiredoxin-5, mitochondrial
- Thioredoxin, mitochondrial
- Sulfiredoxin-1
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
- Thioredoxin reductase 2, mitochondrial
- Fanconi anemia group G protein homolog
- Thioredoxin
- Superoxide dismutase, mitochondrial
- Glutathione peroxidase 1
- Non-selective voltage-gated ion channel VDAC1
Sequence:
MAAAAGRLLWSSVARHASAISRSISASTVLRPVASRRTCLTDILWSASAQGKSAFSTSSSFHTPAVTQHAPYFKGTAVVNGEFKELSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWINTPRKNGGLGHMNITLLSDITKQISRDYGVLLESAGIALRGLFIIDPNGVVKHLSVNDLPVGRSVEETLRLVKAFQFVETHGEVCPANWTPESPTIKPSPTASKEYFEKVHQ
Protein: Serine and arginine rich splicing factor 5 (cDNA FLJ57379, highly similar to Splicing factor, arginine/serine-rich 5) (B4DJK0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSGCRVFIGRLNPAAREKDVERFFKGYGRIRDIDLKRGFGFVEFEDPRDADDAVYELDGKELCSERVTIEHARARSRGGRGRGRYSDRFSSRRPRNDRRNAPPVRTENRLIVENLSSRVSWQVC
Protein: Histone deacetylase 6 isoform A (Histone deacetylase 6, isoform A (EC 3.5.1.98)) (LD43531p) (Q86NK9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSPPIVTRRSAQQAKIQTRAMASKSKTGTTGAATAAGGTGSSSGSISGGFNAADPRKSNKPNAALLEAKRRARNNMLKNQGCGSQESVTDIFQNAVNSKSLVRKPTALIYDESMSQHCCLWDKEHYECPERFTRVLERCRELNLTERCLELPSRSATKDEILRLHTEEHFERLKETSGIRDDERMEELSSRYDSIYIHPSTFELSLLASGSTIELVDHLVAGKAQNGMAIIRPPGHHAMKAEYNGYCFFNNVALATQHALDVHKLQRILIIDYDVHHGQGTQRFFYNDPRVVYFSIHRFEHGSFWPHLHESDYHAIGSGAGTGYNFNVPLNATGMTNGDYLAIFQQLLLPVALEFQPELIIVSAGYDAALGCPEGEMEVTPACYPHLLNPLLRLADARVAVVLEGGYCLDSLAEGAALTLRSLLGDPCPPLVETVPLPRAELAQALLSCIAVHRPHWRCLQLQQTYDCVELQDRDKEEDLHTVLRHWIGGPPPMDRYPTRDTAIPLPPEKLTSNAARLQVLRAETKLSVPSFKVCYAYDAQMLLHCNLNDTGHPEQPSRIQHIHKMHDDYGLLKQMKQLSPRAATTDEVCLAHTRAHVNTVRRLLGREPKELHDAAGIYNSVYLHPRTFDCATLAAGLVLQAVDSVLRGESRSGICNVRPPGHHAEQDHPHGFCIFNNVAIAAQYAIRDFGLERVLIVDWDVHHGNGTQHIFESNPKVLYISLHRYEHGSFFPKGPDGNFDVVGKGAGRGFNVNIPWNKKGMGDLEYALAFQQLIMPIAYEFNPQLVLVSAGFDAAIGDPLGGCKVTAEGYGMLTHWLSALASGRIIVCLEGGYNVNSISYAMTMCTKTLLGDPVPTPQLGATALQKPPTVAFQSCVESLQQCLQVQRNHWRSLEFVGRRLPRDPVVGENNNEDFLTASLRHLNISNDDATAAAGGLAGDRPDCGDERPSGSKPKVKVKTLSDYLAENKEALEQSEMFAVYPLKTCPHLRLLRPEEAPRSLDSGAECSVCGSTGENWVCLSCRHVACGRYVNAHMEQHSVEEQHPLAMSTADLSVWCYACSAYVDHPRLYAYLNPLHEDKFQEPMAWTHGCAWREDGCYATGPDGRDEDDDDDNGAGSSICLRLERNN
Protein: Purine nucleoside phosphorylase 2 (EC 2.4.2.1) (Inosine-guanosine phosphorylase) (Purine nucleoside phosphorylase II) (PNP II) (Xanthosine phosphorylase) (P45563)
Organism: Escherichia coli (strain K12)
Function: The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. This protein can degrade all purine nucleosides including xanthosine, inosine and guanosine, but cannot cleave adenosine, deoxyadenosine or hypoxanthine arabinoside. Has a preference for the neutral over the monoanionic form of xanthosine.
Interaction partners:
- Purine nucleoside phosphorylase DeoD-type
- Xanthosine permease
- HTH-type transcriptional regulator XapR
- Hypoxanthine phosphoribosyltransferase
- Pyrimidine/purine nucleoside phosphorylase
- Xanthine-guanine phosphoribosyltransferase
- Guanine deaminase
- 5'/3'-nucleotidase SurE
- Protein UshA
- Pyrimidine 5'-nucleotidase YjjG
Sequence:
MSQVQFSHNPLFCIDIIKTYKPDFTPRVAFILGSGLGALADQIENAVAISYEKLPGFPVSTVHGHAGELVLGHLQGVPVVCMKGRGHFYEGRGMTIMTDAIRTFKLLGCELLFCTNAAGSLRPEVGAGSLVALKDHINTMPGTPMVGLNDDRFGERFFSLANAYDAEYRALLQKVAKEEGFPLTEGVFVSYPGPNFETAAEIRMMQIIGGDVVGMSVVPEVISARHCDLKVVAVSAITNMAEGLSDVKLSHAQTLAAAELSKQNFINLICGFLRKIA
Protein: Uncharacterized protein Rv2575 (P9WL85)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- 2-dehydropantoate 2-reductase
Sequence:
MTFNEGVQIDTSTTSTSGSGGGRRLAIGGGLGGLLVVVVAMLLGVDPGGVLSQQPLDTRDHVAPGFDLSQCRTGADANRFVQCRVVATGNSVDAVWKPLLPGYTRPHMRLFSGQVGTGCGPASSEVGPFYCPVDKTAYFDTDFFQVLVTQFGSSGGPFAEEYVVAHEYGHHVQNLLGVLGRAQQGAQGAAGSGVRTELQADCYAGVWAYYASTVKQESTGVPYLEPLSDKDIQDALAAAAAVGDDRIQQQTTGRTNPETWTHGSAAQRQKWFTVGYQTGDPNICDTFSAADLG
Protein: Arogenate dehydratase 3, chloroplastic (AtADT3) (EC 4.2.1.91) (Prephenate dehydratase 1) (AtPDT1) (Q9ZUY3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Converts the prephenate produced from the shikimate-chorismate pathway into phenylalanine. Together with GCR1 and GPA1, required for blue light-mediated synthesis of phenylpyruvate and subsequently of phenylalanine (Phe), in etiolated seedlings.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:16415218, ECO:0000269|PubMed:19136569}.
Interaction partners:
- Arogenate dehydrogenase 2, chloroplastic
- Bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase
- Chorismate mutase 2
- Chorismate mutase 1, chloroplastic
- Chorismate mutase 3, chloroplastic
- Arogenate dehydrogenase 1, chloroplastic
- Histidinol-phosphate aminotransferase 1, chloroplastic
- Aspartate aminotransferase 3, chloroplastic
- Tyrosine transaminase family protein
- Probable aminotransferase TAT4
Sequence:
MRTLLPSHTPATVTTAARRRHVIHCAGKRSDSFSINSSSSDWQSSCAILSSKVNSQEQSESLSSNSNGSSSYHVSAVNGHNNGAGVSDLNLVPFNNNQSIQSKKPLSISDLSPAPMHGSNLRVAYQGVPGAYSEAAAGKAYPNCQAIPCDQFEVAFQAVELWIADRAVLPVENSLGGSIHRNYDLLLRHRLHIVGEVQLPVHHCLIALPGVRKEFLTRVISHPQGLAQCEHTLTKLGLNVAREAVDDTAGAAEFIAANNIRDTAAIASARAAEIYGLEILEDGIQDDASNVTRFVMLAREPIIPRTDRPFKTSIVFAHEKGTCVLFKVLSAFAFRNISLTKIESRPNHNVPIRLVDEANVGTAKHFEYMFYIDFEASMAESRAQNALSEVQEFTSFLRVLGSYPMDMTSWSPSSSSSSSSTFSL
Protein: 2310061I04Rik protein (A0PJN6)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
AQALNSLSMVLPPRKREKGPGPELHSGCLDGLRSLFEGPPCPYPGAVIPFQAPGPSHSSPTTPSGDESMEEHLAVMHERLRQELPTLFLRSHDYTIYSMDVEFINEILNIRTKGRTFYVMSLTLCRFLVWNYFAQFRLEILQLTRHPENWTLQARWRLIGLPIHMLFLRFYRRDKEDLYRTFDAFSTFYLNSSGLICRHHLDKLMPSHSPSTPVKKLLVGALVALGLSEPEPSLHLCSKA
Protein: RH27607p (Q8SY87)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSVRHDWYQSETKVVITVLLKNAVDKNYAVEITQKRVHMTADGYELDLKLLHPIVVERSSYKAFSTKVEITLAKETGIRWENLEEAIVAAPVKPKAKNWDQLVSEEEKIDDKEAKGEAALTNLFKKIYSSSSPEVQKAMNKSFSESGGTVLSTNWNEVGKERVTVKPPNGTEFREWEK
Protein: Pre-mRNA-splicing factor CWC24 (Complexed with CEF1 protein 24) (P53769)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in pre-mRNA splicing.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Pre-mRNA-splicing helicase BRR2
- Pre-mRNA-splicing factor CEF1
- Pre-mRNA-splicing factor CWC2
- Pre-mRNA-processing factor 19
- Peptidyl-prolyl isomerase CWC27
- Pre-mRNA-splicing factor SNT309
- Cold sensitive U2 snRNA suppressor 1
- Pre-mRNA-splicing factor PRP11
- Pre-mRNA-splicing factor CWC22
- Pre-mRNA-splicing factor CWC26
Sequence:
MFRKRLVNKSSSDEKNQKKRQKINFSEEKLVASDEEKGSSDLMSLAKSGNSRTLQLSHENEGKLQKKGEDLDKYTLTVNDDSTKEDLLNFERKELAEKAKKRRPSDDNELVLNMSGKNKRLTKQINQPTNIRTTVLMDFQPDVCKDYKQTGYCGYGDSCKFLHSRDDFKTGWKLNQEWNADKEDSKAVTLDLEKIPFKCTLCKEDYKSPVVTNCGHYFCGSCFAKDMKKGTKCFICHKETHGSAKVASDLQKMLNKRKS
Protein: Adhesion G-protein coupled receptor G6 (Developmentally regulated G-protein-coupled receptor) (G-protein coupled receptor 126) (Vascular inducible G protein-coupled receptor) [Cleaved into: ADGRG6 N-terminal fragment (ADGRG6-NTF); ADGRG6 C-terminal fragment (ADGRG6-CTF)] (Q86SQ4)
Organism: Homo sapiens (Human)
Function: G-protein coupled receptor which is activated by type IV collagen, a major constituent of the basement membrane (By similarity). Couples to G(i)-proteins as well as G(s)-proteins. Essential for normal differentiation of promyelinating Schwann cells and for normal myelination of axons. Regulates neural, cardiac and ear development via G-protein- and/or N-terminus-dependent signaling (By similarity). May act as a receptor for PRNP which may promote myelin homeostasis (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:15189448, ECO:0000269|PubMed:15225624, ECO:0000269|PubMed:24227709}; Multi-pass membrane protein {ECO:0000255}. Note=Detected on the cell surface of activated but not resting umbilical vein. {ECO:0000269|PubMed:15225624}.
Interaction partners:
- POU domain, class 3, transcription factor 1
- Aminopeptidase NAALADL1
- L-selectin
- Myotubularin-related protein 13
Sequence:
MMFRSDRMWSCHWKWKPSPLLFLFALYIMCVPHSVWGCANCRVVLSNPSGTFTSPCYPNDYPNSQACMWTLRAPTGYIIQITFNDFDIEEAPNCIYDSLSLDNGESQTKFCGATAKGLSFNSSANEMHVSFSSDFSIQKKGFNASYIRVAVSLRNQKVILPQTSDAYQVSVAKSISIPELSAFTLCFEATKVGHEDSDWTAFSYSNASFTQLLSFGKAKSGYFLSISDSKCLLNNALPVKEKEDIFAESFEQLCLVWNNSLGSIGVNFKRNYETVPCDSTISKVIPGNGKLLLGSNQNEIVSLKGDIYNFRLWNFTMNAKILSNLSCNVKGNVVDWQNDFWNIPNLALKAESNLSCGSYLIPLPAAELASCADLGTLCQATVNSPSTTPPTVTTNMPVTNRIDKQRNDGIIYRISVVIQNILRHPEVKVQSKVAEWLNSTFQNWNYTVYVVNISFHLSAGEDKIKVKRSLEDEPRLVLWALLVYNATNNTNLEGKIIQQKLLKNNESLDEGLRLHTVNVRQLGHCLAMEEPKGYYWPSIQPSEYVLPCPDKPGFSASRICFYNATNPLVTYWGPVDISNCLKEANEVANQILNLTADGQNLTSANITNIVEQVKRIVNKEENIDITLGSTLMNIFSNILSSSDSDLLESSSEALKTIDELAFKIDLNSTSHVNITTRNLALSVSSLLPGTNAISNFSIGLPSNNESYFQMDFESGQVDPLASVILPPNLLENLSPEDSVLVRRAQFTFFNKTGLFQDVGPQRKTLVSYVMACSIGNITIQNLKDPVQIKIKHTRTQEVHHPICAFWDLNKNKSFGGWNTSGCVAHRDSDASETVCLCNHFTHFGVLMDLPRSASQLDARNTKVLTFISYIGCGISAIFSAATLLTYVAFEKLRRDYPSKILMNLSTALLFLNLLFLLDGWITSFNVDGLCIAVAVLLHFFLLATFTWMGLEAIHMYIALVKVFNTYIRRYILKFCIIGWGLPALVVSVVLASRNNNEVYGKESYGKEKGDEFCWIQDPVIFYVTCAGYFGVMFFLNIAMFIVVMVQICGRNGKRSNRTLREEVLRNLRSVVSLTFLLGMTWGFAFFAWGPLNIPFMYLFSIFNSLQGLFIFIFHCAMKENVQKQWRQHLCCGRFRLADNSDWSKTATNIIKKSSDNLGKSLSSSSIGSNSTYLTSKSKSSSTTYFKRNSHTDNVSYEHSFNKSGSLRQCFHGQVLVKTGPC
Protein: Uncharacterized protein (A0A1D8PTJ1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
Sequence:
MSSSVNLSSTREIKNEIAKEDVDGTNSSNIHESTTKIKDNVSSKDNNQHSVNDDNDYDNKTPEQLSKIYEEYRNRFKVAMEKSNQLFESQQNHFITLSYYYRRNQIYLSILNDLYAANEDEINIDEDFGVSRLEDLIAKVPRTKKILTPIIKSIKHSTITDKRDELRIGNYMIEKVSDLINDDLTKYHTNPQSIENWCHRNSVPNLISGNYVPIILDNNNDYNGIEYNLNLNDEGHQGATSSTNTTANSNSNTGSVNNSANTHTRKKRKVESTKK
Protein: Aldehyde reductase Ahr (EC 1.1.1.2) (Zinc-dependent alcohol dehydrogenase Ahr) (P27250)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reduction of a wide range of aldehydes including aliphatic fatty aldehydes (C4-C16), into their corresponding alcohols. Has a strong preference for NADPH over NADH as the electron donor. Cannot use glyceraldehyde or a ketone as substrate. Is a relevant source of NADPH-dependent aldehyde reductase activity in E.coli. The in vivo functions of Ahr has yet to be determined.
Interaction partners:
- Bifunctional aldehyde-alcohol dehydrogenase AdhE
- Probable alcohol dehydrogenase EutG
- Probable alcohol dehydrogenase
- Aldehyde dehydrogenase B
- Alcohol dehydrogenase, propanol-preferring
- Aldehyde reductase YahK
- S-
- NADPH-dependent aldehyde reductase YqhD
- Lactaldehyde reductase
- Uncharacterized oxidoreductase YbbO
Sequence:
MSMIKSYAAKEAGGELEVYEYDPGELRPQDVEVQVDYCGICHSDLSMIDNEWGFSQYPLVAGHEVIGRVVALGSAAQDKGLQVGQRVGIGWTARSCGHCDACISGNQINCEQGAVPTIMNRGGFAEKLRADWQWVIPLPENIDIESAGPLLCGGITVFKPLLMHHITATSRVGVIGIGGLGHIAIKLLHAMGCEVTAFSSNPAKEQEVLAMGADKVVNSRDPQALKALAGQFDLIINTVNVSLDWQPYFEALTYGGNFHTVGAVLTPLSVPAFTLIAGDRSVSGSATGTPYELRKLMRFAARSKVAPTTELFPMSKINDAIQHVRDGKARYRVVLKADF
Protein: Odorant receptor 43b (P81918)
Organism: Drosophila melanogaster (Fruit fly)
Function: Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. May form a complex with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Odorant receptor 47a
Sequence:
MFGHFKLVYPAPISEPIQSRDSNAYMMETLRNSGLNLKNDFGIGRKIWRVFSFTYNMVILPVSFPINYVIHLAEFPPELLLQSLQLCLNTWCFALKFFTLIVYTHRLELANKHFDELDKYCVKPAEKRKVRDMVATITRLYLTFVVVYVLYATSTLLDGLLHHRVPYNTYYPFINWRVDRTQMYIQSFLEYFTVGYAIYVATATDSYPVIYVAALRTHILLLKDRIIYLGDPSNEGSSDPSYMFKSLVDCIKAHRTMLNFCDAIQPIISGTIFAQFIICGSILGIIMINMVLFADQSTRFGIVIYVMAVLLQTFPLCFYCNAIVDDCKELAHALFHSAWWVQDKRYQRTVIQFLQKLQQPMTFTAMNIFNINLATNINVAKFAFTVYAIASGMNLDQKLSIKE
Protein: Putative GroEL-like chaperonine protein (Q2Z0T5)
Organism: Pseudomonas phage EL
Interaction partners:
Sequence:
MSQTLLVHGKDAQGIIKQVLSEVYDAVTSTMGPNGQLVMIKNGVSTKTTKDGVTVARSIRFADEAHELVNRVITEPATKTDEECGDGTTTTIMLTHALYHLFKDFPGFQHHRNIEDLVERVIQRLESMAIRVEVDDPRLYQVALTSSNQDEKLARLVSELYANNKGSYPDIELKEGVNFEDQIEQTTGRTIRMFYANPWFAKGHQGGVTELTGFTAFVIDRRIDKEDTQKLIDGVNHLVKTHKQHLALPILLIARSFEEAANSTLMQLNAAHPTLVEDGRPWLIPLSTPVGGAIGTSELQDIAVMLNAPMLSDVADLTKLDTHSINGQHGQLELGGNRSILKSTTPKDEDRIEQHARGIEELLEGFSLSDKFSVRARYNERRIRTLRGKLITISVGGETYSEVKERVDRYEDVVKAIRSALENGILPGGGVSLVKAVFGTIKEGLEDKDQSAEFAKRYINSGIANELMRLSTIQHKLLFKDTALYKENGSFHFNDDWLNTPTVMNLATGEIGTPEGLGIYDTAYASITALKGGLQTAKILATTKTLILGEKLSAVKVR