wanglab/gogpt-training-data huggingface dataset:
Protein: Fibroblast growth factor receptor-like 1 (Q7T2H2)
Organism: Gallus gallus (Chicken)
Function: Has a negative effect on cell proliferation.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Fibroblast growth factor 8
- Fibroblast growth factor 2
- Uncharacterized protein.
- Fibroblast growth factor
- Fibroblast growth factor 3
- Fibroblast growth factor 10
- Fibroblast growth factor
- Sprouty related EVH1 domain containing 2.
Sequence:
MGLQLALLLAGIVALSDSARGPPRIADKVIHRQSVRLGRTIKLLCPVEGDPPPLTMWMKDGRTIHSGWTRFRILQQGLKIKEVESEDAGTYICKATNGFGSTNVNYTLIVIDDTSSGKNSQTPEGSNGEYEDHSGKQWAQPRFTQPAKMRRRVIARPVGSSIRLKCVASGNPRPDITWLKDNKPLMPHEIGENKKKKWTLNLKNLKPEDSGKYTCRVFNKVGEINATYKVEVIQRTRSKPILTGTHPVNTTVDYGGTTSFQCKVRSDVKPVIQWLKRVEYGTESKYNSTIDVGGQKFVVLPTGEVWSRPDGSYLNKLMITRAKEEDAGMYICLGANTMGYSFRSAFLTVLPDPKPPSAPVPPSSVSSLPWPVIIGIPAGAVFIFGTILLWLCQTKKKPCSPPAAAPVHRPQPRDRICVSQVPDKDCISSINYEEYVAQQQHLLSQGPALAPAMASKMYPKIYTDIHTHTHSHVEGKVHQHQHIQYQC
Protein: Stage IV sporulation protein FA (P26936)
Organism: Bacillus subtilis (strain 168)
Function: Implicated in the coupling of mother cell to forespore gene expression. Required for spore formation at 37 degrees Celsius, but not at 30 degrees Celsius. SpoIVFA plays a central role in both maintaining the SpoIVFA/BofA/SpoIVFB complex and anchoring it to the outer forespore membrane. SpoIVFA brings BofA into close proximity to SpoIVFB, allowing BofA to inhibit SpoIVFB. Increased accumulation of SpoIVFA seems to inhibit the activity of SpoIVFB and thus regulates the activation of sigma-K.
Subcellular location: Forespore outer membrane.
Interaction partners:
- Stage IV sporulation protein FB
- Sigma-K factor-processing regulatory protein BofA
- SpoIVB peptidase
- Carboxy-terminal processing protease CtpB
- Stage II sporulation protein M
- Stage II sporulation protein P
- Stage II sporulation protein Q
- Stage III sporulation protein AH
- Stage II sporulation protein D
- Stage III sporulation protein AG
Sequence:
MSHRADEIRKRLEKRRKQLSGSKRFSTQTVSEKQKPPSWVMVTDQEKHGTLPVYEDNMPTFNGKHPLVKTDSIILKCLLSACLVLVSAIAYKTNIGPVSQIKPAVAKTFETEFQFASASHWFETKFGNPLAFLAPEHKNKEQQIEVGKDLIAPASGKVQQDFQDNGEGIKVETSSDKIDSVKEGYVVEVSKDSQTGLTVKVQHADNTYSIYGELKDVDVALYDFVDKGKKLGSIKLDDHNKGVYYFAMKDGDKFIDPIQVISFE
Protein: CRR41 (A0A178W725)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MASTSTLLLPSLSSKNLHIAVPIRTNSFVRRTTKFSTKCSSNPESKDQFINLTPAPESINTTSAEKFPIEKRRRSEIIRDRTQRGIEKPEPPNFEIGWKRTKEINLEKPKGYVIMDFLEKFEALMAREFGSKELLAKAGEIVAERAREEAEVLRDEGKVEERMVTELFRVLKLMEMDLAMVKASVKDETLSQRIEQARARCRQAILVANSF
Protein: BCL2 like 14 (K7EMX4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGLSPCCPGWFQTPGHSLSSCLSLPKRWDCRPNMCSTSGCDLEEIPLDDDDLNTIEFKILAYYTRHHVFKSTPALFSPKLLRTRSLSQRGLGNCSANESWTEVSWPCRNSQSSEKAINLGKKKSSWKAFFGVVEKEDSQSTPAKVSAQGQRTLEYQDSHSQQWSRCLSNVEQCLEHEAVDPKVISIANRVAEIVYSWPPPQATQAGGFKSKEIFVTEGLSFQLQGHVPVASSSKKDEEEQILAKIVELLKYSGDQLERKLKKDKALMGHFQDGLSYSVFKTITDQVLMGVDPRGESEVKAQGFKAALVIDVTAKLTAIDNHPMNRVLGFGTKYLKENFSPWIQQHGGWEKILGISHEEVD
Protein: Zona pellucida sperm-binding protein 3 (Sperm receptor) (Zona pellucida glycoprotein 3) (Zp-3) (Zona pellucida glycoprotein 3-beta) (Zp-3-beta) (Zp3-beta) (Zona pellucida protein C) [Cleaved into: Processed zona pellucida sperm-binding protein 3] (P42098)
Organism: Sus scrofa (Pig)
Function: Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy. The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP3 is essential for zona matrix formation. May not have a sperm-binding activity by itself but may increase sperm-binding activity of ZPB.
Subcellular location: [Processed zona pellucida sperm-binding protein 3]: Zona pellucida {ECO:0000250|UniProtKB:P21754}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P48833}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Zona pellucida sperm-binding protein 4
- Zona pellucida sperm-binding protein 2
- Oviduct-specific glycoprotein
- Growth/differentiation factor 9
- Beta-1,4-galactosyltransferase
- Factor in the germline alpha
- Hyaluronidase
- Homeobox domain-containing protein.
Sequence:
MAPSWRFFVCFLLWGGTELCSPQPVWQDEGQRLRPSKPPTVMVECQEAQLVVIVSKDLFGTGKLIRPADLSLGPAKCEPLVSQDTDAVVRFEVGLHECGSSLQVTDDALVYSTFLRHDPRPAGNLSILRTNRAEVPIECHYPRQGNVSSWAILPTWVPFRTTVFSEEKLVFSLRLMEENWSAEKMTPTFQLGDRAHLQAQVHTGSHVPLRLFVDHCVATLTPDWNTSPSHTIVDFHGCLVDGLTEASSAFKAPRPGPETLQFTVDVFHFANDSRNTIYITCHLKVTPADRVPDQLNKACSFSKSSNRWSPVEGPAVICRCCHKGQCGTPSLSRKLSMPKRQSAPRSRRHVTDEADVTVGPLIFLGKTSDHGVEGSTSSPTSVMVGLGLATVVTLTLATIVLGVPRRRRAAAHLVCPVSASQ
Protein: Pyruvate decarboxylase (EC 4.1.1.1) (Q6FJA3)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- alcohol dehydrogenase
- Pyruvate kinase 1
- alcohol dehydrogenase
- Pyruvate kinase 2
- Candida glabrata strain CBS138 chromosome D complete sequence
- Aldehyde dehydrogenase
- S-
- alcohol dehydrogenase
- alcohol dehydrogenase
- Fructose-bisphosphate aldolase
Sequence:
MSEITLGRYLFERLNQVDVKTIFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKGMSCIITTFGVGELSALNGIAGSYAEHVGVLHVVGVPSISSQAKQLLLHHTLGNGDFTVFHRMSANISETTAMVTDIATAPAEIDRCIRTTYITQRPVYLGLPANLVDLKVPAKLLETPIDLSLKPNDPEAETEVVDTVLELIKAAKNPVILADACASRHDVKAETKKLIDATQFPSFVTPMGKGSIDEQHPRFGGVYVGTLSRPEVKEAVESADLILSVGALLSDFNTGSFSYSYKTKNIVEFHSDYIKIRNATFPGVQMKFALQKLLNAVPEAIKGYKPVPVPARVPENKSCDPATPLKQEWMWNQVSKFLQEGDVVITETGTSAFGINQTPFPNNAYGISQVLWGSIGFTTGACLGAAFAAEEIDPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGYTIERLIHGEKAGYNDIQNWDHLALLPTFGAKDYENHRVATTGEWDKLTQDKEFNKNSKIRMIEVMLPVMDAPTSLIEQAKLTASINAKQE
Protein: T-complex protein 1 subunit alpha (TCP-1-alpha) (CCT-alpha) (Chaperonin containing TCP1 subunit 1) (P12613)
Organism: Drosophila melanogaster (Fruit fly)
Function: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.
Subcellular location: Cytoplasm.
Interaction partners:
- T-complex protein 1 subunit theta
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit beta
- Chaperonin containing TCP1 subunit 6
- T-complex protein 1 subunit gamma
- Uncharacterized protein
- Phosducin-like protein 2
- 60 kDa heat shock protein homolog 1, mitochondrial
Sequence:
MSTLASPLSIAGTRQSGASVRTQNVMAALSISNIVKSSLGPVGLDKMLVDDIGDVTVTNDGATILRLLEVEHPAAKVLVELAQLQDEEVGDGTTSVVILAAELLKNADELVKQKIHPTSIISGYRIACKEACKYISEHLTAPVDELGRDSLINIAKTSMSSKIIGADAEFFSAMVVDAAQSVKITDPRGQAAYSIKAINVLKAHGKSARESVLIPGYALNCTIASQQMPKKIVNAKIACLDFSLQKTKMKMGVQVLINDPDKLEAIRARELDITKERINMILGTGVNVVLVSGGVDDLCMKYFVEAGAMAVRRVKKSDLKIIAKATGAAFITSLTNMDGEESFDASMVGEAAEVAQERICDDELILIKGTKARAAASIILRGPNDFYCDEMERSVHDALCVVKRVLESKKVVAGGGCVEAALSIYLENFATSLASREQLAIAEFAKSLLVIPKTLSVNAAKDATDLVAKLRSYHNSSQTKPERSDLKWTGLDLIEGVVRDNKKAGVLEPAMSKIKSLKFATEAAITILRIDDMIKLNPEDKSGKSYADACAAGELDG
Protein: Pre-mRNA-splicing factor sap114 (Spliceosome-associated protein 145) (O13900)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in pre-mRNA splicing. May be involved in endoplasmic reticulum-associated protein degradation (ERAD) and required for growth at low and high temperatures (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Pre-mRNA-splicing factor dre4
- Pre-mRNA-splicing factor sap145
- Pre-mRNA-splicing factor sap61
- Spliceosome-associated protein 49
- Pre-mRNA-splicing factor sap62
- Pre-mRNA-splicing factor cdc5
- Pre-mRNA-splicing factor prp1
- Pre-mRNA-splicing factor prp12
- U2 small nuclear ribonucleoprotein A'
- U2 snRNP component prp10
Sequence:
MSSLMEFQDRNTTNNETEHQKSITDQSSSVPAGVILPPPAIREIIDKSASYVARNGPAFEEKIRQNEQANTKFAFLHANDPYHPYYQHKLTEAREGKLKSHATGLSTQKTSTLARPIQKPIEATIPAPSPYLFSEPLPSISSLDLDVLRLTARYAAVRGSSFLVSLSQKEWNNTQFDFLKPNNALYPYFMRIVQQYTSLIREPISSPEQELRENVRDPYSLLSKIQPRVRWQSHMESQKKKQKEEAEKEKLEYAQIDWNDFVVVEVIQFTKSDEHAKLAKPTNLADLQTATLEQKSAMFTMPDQNYTIEEAPPTAEPWEPISAPKKQEFGVSLPPSLASPEKGGISSTTSVSPAAQASPVLSTTTQPKVQKPVPKAFQPKVPMEISPFSGELVPATELEEHMRLKLLDPRWQEQRKVEESRKSTLNLENVNVAANMKRLVSQRTDLFDVQNGVEISQEEIERRKRAATQSAWGATPTNKRR
Protein: Glucuronokinase with putative uridyl pyrophosphorylase (F6NZ60)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Aldo-keto reductase family 1 member A1-B
- Inositol oxygenase
- Klotho
- Aldo-keto reductase family 1 member A1-A
- Beta-glucuronidase
- Hexosyltransferase
- UDP-glucose 6-dehydrogenase
- Aldo-keto reductase family 1, member B1
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1
- Exostosin-like 3
Sequence:
MICILLVAGHGTVLETQIKNDVSGLYAHLTGVPKALLPGVGGKKILDFWWEAVNTRQLFSEVYLVTNADKYKHYERWATANDFPVENVVNDGSTTLDDRLGAVADVELAIRSRQLQDDIMVIAGDMLCSDQNFDIAQVIRFFRSKPGELAIYYELESGEKSYSRGIVKVCPNTHRVTRFLEKPQEGVTASRLASVVFYCLRKESLTYISEFLNKHPDVKDRTFGKFWEWLVNEEKVPVYGMKLPTGFQLIGQVGLSDYTKWLAHYSSKQQLSPSKPITCRSYARVGLMGNPSDGFNGKTIAMSISNFWAEVTLMESQTLVLLPHPLNDPTEFGGLQDLFRISRKEGYLGGLRLLQATCKKFYQFCSEQGIALSKQNFTLKYDTNIPRQVGLAGSSAIVSATLKCLMKFYNITDNDLPQPVRANFILNVETDELFITAGLQDRVVQVYEGLVYMDFSKQLMDERGYGEYIPLDMRDLPMFWLAYLSDPSDSGRIHSNVRQRWLNGEPAVVEAMKSFAELTDQSRAAFQCKDWARLAQLMDENFELRRSVYTDDCLGPGNLKMVQLARQFGSAVKLPGSGGAVVGLCMDQERLMEMKRAFQEAGCVFCLIVPYDPSVQGQN
Protein: aromatase (EC 1.14.14.14) (Cytochrome P-450AROM) (Estrogen synthase) (Q8JG19)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
Sequence:
MATSIVDDTSVSGVLLLLLCLLLITAWCLTNASHIPGPFFWAGLGPILSYSRFIWSGIGTACNYYNKRYGSMVRVWINGEETLILSKSSAVYHVLKSAHYTARFASKRGLQCIGMDGRGIIFNSDIPLWKKMRTYFAKALTGPGLQRTVGICVSATDRHLERLQEMTDPSGHVDVLNLLRCIVVDISNKLFLRVPLNEKELLLKIQHYFDTWQTVLIKPDIFFKCGWMYKRHQQAAKELQDVMESLIETKRRIISEAEKLDDDIDFTSELIFAQNHGELSADDVRQCVLEMVIAAPDTLSISLFFMLMLLKQNPEVEMRIVEEISTLMGENDVMTVDFQNFRVLESFINESMRFHPVVDFTMRKALEDDVIDGTKVSKGTNIILNIGLMHKTEFFPKPNEFSLENFDKTVPSRFFQPFGCGPRSCVGKHIAMMMMKAVLVTLLSRYTVCPRHGNTLSSIRQTNNLSQQPVEDEHSLAMRFIPRQMTMT
Protein: 2-hydroxymuconate tautomerase (EC 5.3.2.6) ((2Z,4E)-2-hydroxyhexa-2,4-dienedioate keto-enol isomerase) (4-oxalocrotonate tautomerase) (4-OT) (P70994)
Organism: Bacillus subtilis (strain 168)
Function: Catalyzes both 1,3- and 1,5-keto-enol tautomerization of the diacid 2-hydroxymuconate (2-hydroxy-2,4-hexadienedioate) to produce 2-oxo-4-hexenedioate. This reaction is highly stereoselective and produces a mixture of stereoisomers, where the (3S)-isomer of 2-oxo-4-hexenedioate predominates. Also catalyzes the tautomerization of 2-hydroxymuconate to 2-oxo-3-hexenedioate, however this reaction is slower and occurs after the tautomerization of 2-hydroxymuconate to 2-oxo-4-hexenedioate. Using 2-hydroxy-2,4-pentadienoate, phenylenolpyruvate, (p-hydroxyphenyl)-enolpyruvate and 2-hydroxy-2,4-heptadiene-1,7-dioate, YwhB is a highly efficient 1,3-keto-enol tautomerase, but clearly not a 1,5-keto-enol tautomerase. Tautomerization of the two monoacids 2-hydroxy-2,4-pentadienoate and phenylenolpyruvate produces a mixture of stereoisomers, where the (3R)-isomers predominate.
Interaction partners:
- Catechol-2,3-dioxygenase
- 5'-nucleotidase YutF
Sequence:
MPYVTVKMLEGRTDEQKRNLVEKVTEAVKETTGASEEKIVVFIEEMRKDHYAVAGKRLSDME
Protein: Annexin A3 (35-alpha calcimedin) (Annexin III) (Annexin-3) (Inositol 1,2-cyclic phosphate 2-phosphohydrolase) (Lipocortin III) (Placental anticoagulant protein III) (PAP-III) (P12429)
Organism: Homo sapiens (Human)
Function: Inhibitor of phospholipase A2, also possesses anti-coagulant properties. Also cleaves the cyclic bond of inositol 1,2-cyclic phosphate to form inositol 1-phosphate.
Interaction partners:
Sequence:
MASIWVGHRGTVRDYPDFSPSVDAEAIQKAIRGIGTDEKMLISILTERSNAQRQLIVKEYQAAYGKELKDDLKGDLSGHFEHLMVALVTPPAVFDAKQLKKSMKGAGTNEDALIEILTTRTSRQMKDISQAYYTVYKKSLGDDISSETSGDFRKALLTLADGRRDESLKVDEHLAKQDAQILYKAGENRWGTDEDKFTEILCLRSFPQLKLTFDEYRNISQKDIVDSIKGELSGHFEDLLLAIVNCVRNTPAFLAERLHRALKGIGTDEFTLNRIMVSRSEIDLLDIRTEFKKHYGYSLYSAIKSDTSGDYEITLLKICGGDD
Protein: Uncharacterized protein (Q3UWX6)
Organism: Mus musculus (Mouse)
Interaction partners:
- Nucleoplasmin-2
Sequence:
MSPVLWQQQLLLEHSISTSEFISNHVFNAEEQSKVEGSWTSISVQSSKEEVVLGRPAPTTGQLHFMRNCICNIRHHVTAADLNRKTTEASKNLKMLEEEIGFYRNLHSQLRMAQAQLKNKVNMLKQENRRIWGRCATLQQNLEELKMIYKNQLEDTSDPQTQQQQDPERTEELLQDSHKQKKLGIQEKNLAEKQQYYFEVRRKSHLYSCFLTELNQLKKKLEMLSQENKEMQGDCALLQHHVEDLKPIYKKQQEEDSDLQTQHQKHMERMEEKLQYMLKKKNMAIKQRELAEKLKYQFEVLQMRFDKLQQEMELAIAQEERVLQKDLLHQEPPAEPHPQKPQDPLGGFALT
Protein: beta-N-acetylhexosaminidase (EC 3.2.1.52) (G5EDG9)
Organism: Caenorhabditis elegans
Interaction partners:
- Alpha-
- Beta-1,4-galactosyltransferase galt-1
- Alpha-
- Alpha-
- Beta-hexosaminidase A
- Alpha-galactosidase
- Alpha-mannosidase
- Exostosin-like-3 homolog
Sequence:
MLRGFFGRRSRSAWVRLIYLCIVTIIFLFATSQFKSTTTHARFVPEPSDPRLHPNSPLQAPKAQEPAAAETTKKPSRQPHHTTAKPRTENVEINGEKYPKLSPDGNLIPQRRIVHLDLKGAPYKPEFFTELFAFFNRIQATGILLEWEDMFPFKGRLRGAINKNAYSMETVEHILQEAQKHHLQIIPLVQTMGHLEWILKLEEFAHLREDTRFPQVICFSDENAWELIKEMIEEVANVHKKYGMSYFHIGADEAFQIGICNASITQIKKEFTRERLMLWHIARTARFVKEKYPETQVLAWHDMLASAMESDIEDYKLTELLQPVLWNYAEDLDIYLPRSTWMILRNFRNVWGSSAWKGADGPARYSTNANHYLKNHESWIKQFTMVYKDFEVVEGLIMAGWSRYDHFAVLAETIPVALPTLAMSMETMIEGRPLAGNYPVTSELLQCTPPLDLGFTATGCKFPGNRIYELINEMYQKQMQLRTYRLDDYELNGWLSRVADDYSVSSHWYIDKIENMIEMHATPLEQLADDLRFEMERIFFKDTVDEFIFTYLGEDLEWFNRKRETIRKVSTSQTFPKRPFIESAKSEKTCT
Protein: Catabolite repressor-activator, DNA-binding transcriptional dual regulator (Q88PQ6)
Organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
Interaction partners:
- phosphoenolpyruvate--protein phosphotransferase
- protein-N
- Phosphofructokinase
- Hydrolase
- Fructose-1,6-bisphosphatase class 1
- Glyceraldehyde-3-phosphate dehydrogenase
- Glutamate synthase large chain
Sequence:
MKLSDIARLAGVSVTTASYVINGKAEQQRISNSTVERVRAVVEAHGFTPNPQAAGLRSRHTRTLGFILPDLENPSYARIAKQLEQGARARGYQLLIASSDDQPDSERQLQQLFRARRCDALFVASCLPPEDDSYRELQDKGLPVIAIDRRLDPAHFCSVISDDRDASRQLAASLLSSAPRSIALIGARPELSVSQARAGGFDEALQGYTGEVRRYQGEAFSRECGQRLMQQLIDDLGGLPDALVTTSYVLLQGVFDTLQARPVDSRQLQLGTFGDNQLLDFLPLPVNAMAQQHGQIAATALELALAAIEEKRYEPGVHAVGRTFKQRISVA
Protein: Interferon gamma (IFN-gamma) (A9QXB7)
Organism: Bos taurus (Bovine)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|PIRNR:PIRNR001936}.
Interaction partners:
Sequence:
MKYTSYFLALLLCGLLGFSGSYGQGQFFREIENLKEYFNASSPDVAKGGPLFSEILKNWKDESDKKIIQSQIVSFYFKLFENLKDNQVIQRSMDIIKQDMFQKFLNGSSEKLEDFKKLIQIPVDDLQIQRKAINELIKVMNDLSPKSNLRKRKRSQNLFRGRRAST
Protein: Short-chain dehydrogenase/reductase family protein (Q54BI7)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- CRAL-TRIO domain-containing protein DDB_G0278031
Sequence:
MNKLNNKVAIITGGSDGIGKETCKIIAREIGTIVIGCRNKQKGEVAAKEISSHTGNSNIIILDLDLSKQNSVKSFVNEFNKLNLPLDLLINNAGVMCPPFSITQDGYSFQIATNHFGPFLLTNLLLKNLEKSENPRILVLTSDRFKDADLSLILNDKINVESEANYNQLKDYSLSKCCNLLFTKELQRKLIEKGSKIVVNSINPGKVQTSLQRDFTGILKVAFSLMPNFIFTPIQVASKECAKVALGTDPSLNGIKGSYFNIGVLTETPRQFNSIEISKKLWDITSKFTNISNDLVLK
Protein: Ferredoxin (P83585)
Organism: Solanum abutiloides (Cyphomandra abutiloides)
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:12620316}.
Interaction partners:
Sequence:
ATYKVKLVTPDGPVEFECPDDEYILDRAEEEGHDLPYSCRAGSCSSCAGKIAAGSVDQSDGNFLDDDQIADGFVLTCVAYPQSDVTIETHKEEELTA
Protein: Synaptotagmin-5 (Synaptotagmin IX) (Synaptotagmin V) (SytV) (Q9R0N5)
Organism: Mus musculus (Mouse)
Function: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Regulates the Ca(2+)-dependent secretion of norepinephrine in PC12 cells. Required for export from the endocytic recycling compartment to the cell surface.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:11751925}; Single-pass membrane protein {ECO:0000269|PubMed:11751925}. Recycling endosome membrane {ECO:0000269|PubMed:11751925}; Single-pass membrane protein {ECO:0000269|PubMed:11751925}. Note=In mast cells, localizes to the endocytic recycling compartment.
Interaction partners:
- Syntaxin-1A
- Synaptosomal-associated protein 25
- Vesicle-associated membrane protein 2
Sequence:
MFPEPPTLGSPAPKTPPDSSRIRQGAVPAWVLATIVLGSGLLVFSSCFCLYRKRCRRRMGKKSQAQAQVHLQEVKELGRSYIDKVQPEIEELDRSPSMPGQQVSDKHQLGRLQYSLDYDFQTGQLLVGILQAQGLAALDLGGSSDPYVSVYLLPDKRRRHETKVHRQTLNPHFGETFAFKVPYVELGGRVLVMAVYDFDRFSRNDAIGEVRVPMSSVNLGRPVQAWRELQVAPKEEQEKLGDICFSLRYVPTAGKLTVIVLEAKNLKKMDVGGLSDPYVKVHLLQGGKKVRKKKTTIKKNTLNPYYNEAFSFEVPCDQVQKVQVELTVLDYDKLGKNEAIGRVAVGAAVGGAGLRHWADMLANPRRPIAQWHSLRPPDRARPIPAP
Protein: Probable tRNA(Ile)-lysidine synthase (EC 6.3.4.19) (tRNA(Ile)-2-lysyl-cytidine synthase) (tRNA(Ile)-lysidine synthetase) (Q10441)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine (By similarity).
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Cytoplasmic tRNA 2-thiolation protein 2
- RCC1 repeat-containing protein C10F6.04
- tRNA modification GTPase mss1
- Probable 3-mercaptopyruvate sulfurtransferase
- Probable tRNA-splicing endonuclease subunit sen54
Sequence:
MDTIKLKEFYNSLVSIRRRVGHRRLGIAVSGGVDSMLLSWFMKESQIMFGWPNQFIAFVVDHRIRKNSTEEALQTIWNLNRMLIPNVYLNINWGNDDVHSLTNLETIAREHRYQVLTRACITHNIRHICTAHHANDQAETIFMRLLRRKPGTWGGLCAMKPVSQIPESDSICGASNIELLRPLLPYYKNQILNTAKQHGIAWEEDPTNADINLTPRNAIRRFLNQHAALTVEATKLATAFQSLQVNIDNKVDEILKDNIVSYHQPSGTLSLCFSKNELKKHSNLTKEELLLRCLTLTTSCRQIKRSSVVSLCNSVFDGKKLTIAKCLLTSSSIKDDTKLQLQISRQPFSKAELKKKTITINPDRYVLWDHRFWIKYSCKNTQTTLILRPLLSKDLNSLKGFLSKEEFLKFCIQVPGHIRFTIPVLSEENDKLVGIPTFGFNFRSDIISNCLHKFKL
Protein: LD08669p (Slimb) (Supernumerary limbs, isoform A) (Supernumerary limbs, isoform C) (Q9VDE3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MMKMETDKIMDETNSNAQAFTTTMLYDPVRKKDSSPTYQTERELCFQYFTQWSESGQVDFVEHLLSRMCHYQHGQINAYLKPMLQRDFITLLPIKGLDHIAENILSYLDAESLKSSELVCKEWLRVISEGMLWKKLIERKVRTDSLWRGLAERRNWMQYLFKPRPGQTQRPHSFHRELFPKIMNDIDSIENNWRTGRHMLRRINCRSENSKGVYCLQYDDGKIVSGLRDNTIKIWDRTDLQCVKTLMGHTGSVLCLQYDDKVIISGSSDSTVRVWDVNTGEMVNTLIHHCEAVLHLRFNNGMMVTCSKDRSIAVWDMTSPSEITLRRVLVGHRAAVNVVDFDEKYIVSASGDRTIKVWSTSSCEFVRTLNGHKRGIACLQYRDRLVVSGSSDNSIRLWDIECGACLRVLEGHEELVRCIRFDTKRIVSGAYDGKIKVWDLVAALDPRAASNTLCLNTLVEHTGRVFRLQFDEFQIVSSSHDDTILIWDFLNFTPNENKTGRTPSPALMEH
Protein: Protein ral2 (P15258)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Essential for mating and for recognition of the mating pheromone, and for the determination of cell shape. Implicated in activation of the ras1 protein.
Interaction partners:
- Ras-like protein 1
- Mei4-dependent protein 6
- Suppressor of kinetochore protein 1
- Uncharacterized protein C2D10.19c
- Rho guanine nucleotide exchange factor scd1
- Protein scd2/ral3
Sequence:
MSEVKRNISLRNSTNIFTSTFSLSSNNVPKPLIGESVIKYGDEAFVYGGRDALNAQLVNDMYVVDLNTCSWKQVEYQGNQKPIPRYFHSGDLWNNKLIFFGGMGFNDDTKCLYVLNDIDIYDIETKQWSHIPGMITENQTNDDAKEVNGSDVDEKSKHLYPSARYGHLHCVLDHYLIIFCGQDLSNSYIEEINIFDLDSGKWVFKSLFNHHCGIYRSNCVVINKDSEFLQMCRPINTTQDSNEHSIGSLFFYLNYNFVNVKRQVIYLELFELDTAESEKKSAALAKDNNQSFRFLELDVTEKFLSSAMPPGLRFPAVNILGDNLILSGIYLTSSRQAFVLWVYSLDKELWLQLDMLGVLNHGSWFKCLVLDCTNRFVVFGNKTRKLTQDYNLRQSNYDHIVFIELEGYGVYRKPQMGRVTERSEQLGKLLLNGISDMEILTIERMHIPCLSRMLYKRWPAFQKIMDRAVEKNQEAFQAEVSQLGPQLTDLPFSSIHSTGSRALYMPYSFETCSAFLHYIYCGTLNGSYCTAKNLCNLLILCKGFEGLETFFAYIVHLLHGVLNRNNVKLIYETAALTGAKGLQLRALRRIARIEQGGTAISPTSPLPNLDD
Protein: Inner membrane protein YgaP (P55734)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- HTH-type transcriptional regulator YgaV
Sequence:
MALTTISPHDAQELIARGAKLIDIRDADEYLREHIPEADLAPLSVLEQSGLPAKLRHEQIIFHCQAGKRTSNNADKLAAIAAPAEIFLLEDGIDGWKKAGLPVAVNKSQPLPLMRQVQIAAGGLILIGVVLGYTVNSGFFLLSGFVGAGLLFAGISGFCGMARLLDKMPWNQRA
Protein: Endoglucanase 8 (EC 3.2.1.4) (Cellulase 1) (AtCEL1) (Endo-1,4-beta glucanase 8) (Q9CAC1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for cellulose formation of the cell wall.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Beta-glucosidase 1
- Putative beta-glucosidase 2
- Putative beta-glucosidase 6
- Endonuclease 1
- Beta-glucosidase 44
- Beta-glucosidase 33
- Probable pectinesterase/pectinesterase inhibitor 44
- 2-oxoglutarate
Sequence:
MARKSLIFPVILLAVLLFSPPIYSAGHDYRDALRKSILFFEGQRSGKLPPDQRLKWRRDSALRDGSSAGVDLSGGYYDAGDNIKFGFPMAFTTTMLSWSIIDFGKTMGPELRNAVKAVKWGTDYLLKATAIPGVVFVQVGDAYSDHNCWERPEDMDTLRTVYKIDRAHPGSDVAGETAAALAAASIVFRKRDPAYSRLLLDRATRVFAFANRYRGAYSNSLYHAVCPFYCDFNGYQDELLWGAAWLHKASRKRAYREFIVKNEVILKAGDTINEFGWDNKHAGINVLISKEVLMGKAEYFESFKQNADGFICSILPGISHPQVQYSRGGLLVKTGGSNMQHVTSLSFLLLAYSNYLSHAKKVVPCGELTASPSLLRQIAKRQVDYILGDNPMGLSYMVGYGQKFPRRIHHRGSSVPSVSAHPSHIGCKEGSRYFLSPNPNPNLLVGAVVGGPNVTDAFPDSRPYFQQSEPTTYINAPLVGLLGYFSAHSTWR
Protein: ATP-sensitive inward rectifier potassium channel 10 (Potassium inwardly rectifying channel subfamily J member 10a) (E7FD27)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003822}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003822}.
Interaction partners:
- Potassium inwardly rectifying channel subfamily J member 16.
- Oligodendrocyte myelin glycoprotein a.
- KN motif and ankyrin repeat domains 1b.
Sequence:
MTSATPPSSRSSSPQKVCHSQTQTDVLKPLLGGGGGGTSTGNGPAALRRRRRVLSKDGRSNVRIEHVSGRGTLYLRDLWTTFLDMQWRYKLFLFSATFAGTWFVFGVLWYLVALVHGDLLEFDPPSNHTPCVMQVQTLTGAFLFSLESQTTIGYGFRCITEECPLAIILLIVQLVITMVMEIFITGTFLAKVARPKKRGETVKFSQHAVVANHEGRPCLMIRVANMRKSLLLGCQVSGKLLQTSQTKEGETVRLDQRNVAFQVDTSSDSPFLILPLTFYHVIDDNSPLRAWAAKGGGWTDPELADFELLVIMSATVEPTSATCQVRTSYLPDEILWGYEFPPVVSLSPSGKYVADFAFFDKVAKTKTPPLFKQAPPSHTQTPQHQGSGEKGADTEKMRLEESYREERGRDRGRVRDQLSVRISNV
Protein: DUF4129 domain-containing protein (P72005)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Possible integral membrane protein
- ABC transporter ATP-binding/permease protein Rv1747
Sequence:
MPGGVCSGRPWGRPWWHPGLVGLLIRLAELLVVMLPLIGVLYVGIKALSSFTRRLGEASGDLASDSPAMPRPTTVENDAARWRAITRAVEAHERTDARWLEYELDAAKLLDFPVMTDMRDPLTTAFHKAKLQADFHKPLRAEDLLDDPDAAGHYLDAVRDYVTAFDTAEAEAMRRRRTGFSREEQQRLARAQSLLRVASDAGATAQERERAYRLARTELDGLIVLPDRTRAGIERGIAGELDD