wanglab/gogpt-training-data huggingface dataset:
Protein: Trabuco, isoform C (Trabuco, isoform D) (Q8IQ30)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVQGNADGSDYKERLIASVKKEVKQLMEEAVTKKYVHEESSSVTSLCGAVEACLSQGLRRRALGLFKTSSTTALLHKIAKSCPEAEHISKLVQEIEASDPSKRSSSSSDSFQRPPMLKKSSSNSMSTGTNAAASTSSASASISVSASTSSMSLASMKYLWIRLALYEKRLTKIIEYLVSNASSFYDRDSLVADSDYGSILSSLLVGPCALEFTRAKTADHYWTDPHADELVQRHRISSCRRSSSTCSRPAIINFKRSLNTSSDEAGTGSFKSIASASVAKDYVESLHQNAKATLLYGKNNVQVLPKDVAEPMPGYLSLHQHIQTLTIKWTPNQLMNGYTEAEEAEDIDKDAFWAYALNINVDEIVYVHCHQSRGEDSGGTVILVGQDGVQRPPIHFPEGGHMQQFLSCLETGLLPHGQLDPPLWSQRGIGKMFLWPRSMRRRILPSVMESVDETPIDYVFRIVSKSRHEEFAATHSILDFVRSTPRRAQLSSCSTTGSSDCSNKSLSIDQFPMESPLILQQQQQQQQQLLQAQSTSIEMVCSTMRRQIISRAFYGWLAYCRHLSTVRTHLSGLVHGRITPEMKADEEGLTKERWQLLNVNGVLENATEFYRLVYFGGVQPELRQEVWPYLLGHYAFGSTTEDRKKQDETCKHYYETTMSEWLAVDAIVQQREKEKTARAVAKLSSGSNSGNDRTVRAADLEAGGDLENEVFEDISDISDPGDLEFDEQQQQQQQQAECAVSGNHLTVKPIPRAMKTSTDSGHVDESFNELDEPDEEDNKQKQQQDEKISESESKLPDYRKLEEQINQEPSCSASTASSYETVGPGEVHQRPNSDTRSVLSPEYLSADDLQLPDDEDAVRPPPPPAAAAVIITKASVDITNWERSPKAAEGDQMSPLEEQAGESGGAGVNMDALQQPKSACASPASSNGGVYSSELLEQFGLNLHRIEKDVQRCDRNYWYFANENLDKLRNVISTYVWEHLDVGYMQGMCDLVAPLLVIFDDESLSYSCFCKLMERMIENFPSGGAMDMHFANMRSLIQILDSEMYDLMDSNGDYTHFYFCYRWFLLDFKRELVYDDVFATWEVIWAAKHIASGHFVLFLALALLETYRDIILSNSMDFTDVIKFFNEMAERHNAQSVLQLARSLVLQLQMIIENK
Protein: Guanine nucleotide-exchange factor SEC12 (Mammalian guanine nucleotide exchange factor Sec12) (mSec12) (Prolactin regulatory element-binding protein) (Q9WTV0)
Organism: Rattus norvegicus (Rat)
Function: Guanine nucleotide exchange factor that specifically activates the small GTPase SAR1B. Mediates the recruitment of SAR1B and other COPII coat components to endoplasmic reticulum membranes and is therefore required for the formation of COPII transport vesicles from the ER.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11422940}; Single-pass membrane protein {ECO:0000269|PubMed:11422940}. Nucleus {ECO:0000269|PubMed:10194769}. Note=Concentrates at endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER). {ECO:0000250|UniProtKB:Q9HCU5}.
Interaction partners:
- Small COPII coat GTPase SAR1B
- MIA SH3 domain ER export factor 2
- Protein SEC13 homolog
- Protein transport protein SEC23
- SEC24 homolog C, COPII coat complex component
- SEC24 homolog A, COPII coat complex component
- SEC24 homolog D, COPII coat complex component
- SEC24 homolog B, COPII coat complex component
- Protein ERGIC-53
- Protein transport protein sec16
Sequence:
MGRRRGVELYRAPFPLYALRIDPKTGLLIAAGGGGAAKTGIKNGVHFLQLEQISGCLSASLLHSHDTETRATMNLALAGDILAAGQDAQCQLLRFQIHQQKGSKAEKSGSKEQGPRQRKGAAPAEKKSGAEVHPEGVELKVKNLEAVQTDFSTEPLQKVVCFNHDNTLLATGGSDGHVRVWKVPSLEKVLEFKAHEGEIGDLALGPDGKLVTVGWDFKASVWQKDQLVTQLQWQENGPTSSNTPYRYQACRFGQVPDQPGGLRLFTVQIPHKRLRQPPPCYLTAWDSSTFLPLQTRSCGHEVISCLTVSESGTFLGLGTVTGSVAIYIAFSLQRLYYVKEAHGIVVTDVTFLPEKGCGPKLLGPHETALFSVAVDSRCQLHLLPSRRSVPVWLLLLLCVGLIIVTILLLQSAFPGFL
Protein: Interleukin 15 receptor subunit alpha (F1M293)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Interleukin-15
- Interleukin 2 receptor, gamma, isoform CRA_a.
- Interleukin-2 receptor subunit beta
- Interleukin-2
- Interleukin-7
- Interleukin-2 receptor subunit alpha
- Interferon gamma
- Interleukin 9
- Tyrosine-protein kinase JAK3
- Granulocyte colony-stimulating factor
Sequence:
KGRSPARTGITCPTPISIEHADIRVKNYSVNSRERYVCNSGFKRKAGTSTLTECVINKNTNVAHWTTPNLKCIRDPSLAHYSPVPTVVTPKVTSQPESLSPPEKEPEALSPKSDTTVATETAIVPGSRLTPSQAASAGTTGTGRHKSSPAPSLATTMTLEPTASTSLRITEISPHSSEMTKVAIPTSVLLVAAGIGLVFLTRYIKSRQASQPRRVEVETMETVPMTVRARSKEDEDHTTSETQGDQPTRGV
Protein: ADP,ATP carrier protein 1 (ADP/ATP translocase 1) (P19568)
Organism: Rickettsia prowazekii (strain Madrid E)
Function: Provides the rickettsial cell with host ATP in exchange for rickettsial ADP. This is an obligate exchange system. This energy acquiring activity is an important component of rickettsial parasitism.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MSTSKSENYLSELRKIIWPIEQYENKKFLPLAFMMFCILLNYSTLRSIKDGFVVTDIGTESISFLKTYIVLPSAVIAMIIYVKLCDILKQENVFYVITSFFLGYFALFAFVLYPYPDLVHPDHKTIESLSLAYPNFKWFIKIVGKWSFASFYTIAELWGTMMLSLLFWQFANQITKIAEAKRFYSMFGLLANLALPVTSVVIGYFLHEKTQIVAEHLKFVPLFVIMITSSFLIILTYRWMNKNVLTDPRLYDPALVKEKKTKAKLSFIESLKMIFTSKYVGYIALLIIAYGVSVNLVEGVWKSKVKELYPTKEAYTIYMGQFQFYQGWVAIAFMLIGSNILRKVSWLTAAMITPLMMFITGAAFFSFIFFDSVIAMNLTGILASSPLTLAVMIGMIQNVLSKGVKYSLFDATKNMAYIPLDKDLRVKGQAAVEVIGGRLGKSGGAIIQSTFFILFPVFGFIEATPYFASIFFIIVILWIFAVKGLNKEYQVLVNKNEK
Protein: Protein AIR1 (Arginine methyltransferase-interacting RING finger protein 1) (P40507)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the TRAMP (TRF4) and TRAMP5 complexes which have a poly(A) RNA polymerase activity and are involved in a post-transcriptional quality control mechanism limiting inappropriate expression of genetic information. Polyadenylation is required for the degradative activity of the exosome on several of its nuclear RNA substrates like cryptic transcripts generated by RNA polymerase II and III, or hypomethylated pre-tRNAi-Met. Both complexes polyadenylate RNA processing and degradation intermediates of snRNAs, snoRNAs and mRNAs that accumulate in strains lacking a functional exosome. AIR1 also inhibits the methylation of NPL3 mediated by HMT1 through its interaction with HMT1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Poly
- ATP-dependent RNA helicase DOB1
- Poly
- Poly
- Protein AIR2
- Exosome complex exonuclease RRP6
- Nuclear polyadenylated RNA-binding protein 3
- Exosome complex exonuclease DIS3
- Probable E3 ubiquitin-protein ligase HUL4
- Exosome complex protein LRP1
Sequence:
MSTLLSEVESIDTLPYVKDTTPTGSDSSSFNKLLAPSIEDVDANPEELRTLRGQGRYFGITDYDSNGAIMEAEPKCNNCSQRGHLKRNCPHVICTYCGFMDDHYSQHCPKAIICTNCNANGHYKSQCPHKWKKVFCTLCNSKRHSRERCPSIWRSYLLKTKDANQGDFDFQTVFCYNCGNAGHFGDDCAERRSSRVPNTDGSAFCGDNLATKFKQHYFNQLKDYKREASQRQHFDNEHEFNLLDYEYNDDAYDLPGSRTYRDKMKWKGKVQSTRNKNSSNNRYESSNNRKKKSPFSAQNYKVTKNKRVQTHPLDFPRSSQNNRTNDYSSQFSYNRDDFPKGPKNKRGRSSSNKSQRNGRY
Protein: Vacuolar iron transporter homolog 2 (Protein NODULIN-LIKE 2) (Vacuolar iron transporter-like 2) (AtVTL2) (Q9SRD3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable vacuolar iron transporter involved in the transfer of iron ions from the cytosol to the vacuole for intracellular iron storage. Involved in regulation of cellular iron homeostasis. Vacuolar iron storage is required for seed embryo and seedling development.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:25360591}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- WAT1-related protein At4g01440
- DUF21 domain-containing protein At5g52790
- At5g23760
- Receptor protein kinase-like protein
- Sulfite exporter TauE/SafE family protein 2
- AT3g19030/K13E13_15
- GRAS family transcription factor family protein
- Cation-chloride cotransporter 1
- RING-H2 finger protein ATL11
- Solute carrier family 40 member 2
Sequence:
MDQSGSNTNMDIEKESTTFDYSKRSQWLRAAVLGANDGLVSTASLMMGVGAVKHDVKAMILSGFAGMVAGACSMAIGEFVSVYSQYDIEVAQMERDSVEIEKEKLPSPMQAAAASALAFSAGAIVPLLAAAFVKEYKMRIISVVVAVTVALMVFGWLGAALGKAPAVRSSARVLFGGWLAMAVTFGLTKLIGLYGL
Protein: Bouquet formation protein 3 (O74510)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Connects telomeres to the nuclear envelop (NE) during both vegetative growth and meiosis. This connection ensures clustering of telomeres to the spindle pole body (SPB) when cells enter meiotic prophase.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:19948484}; Multi-pass membrane protein {ECO:0000255}. Nucleus inner membrane {ECO:0000269|PubMed:19948484}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Bouquet formation protein 4
- DNA-binding protein rap1
- Telomere length regulator taz1
- Lap-Emerin-Man domain protein 2
- Telomere bouquet protein 1
- Telomere bouquet protein 2
- Meiotically up-regulated gene 61 protein
Sequence:
MSGSKCCSSSNTIKVSIYLFLHTLTYGLLNYHLNPRLLASTGVVESDIPYWMSYLSIIMHVGQSLLLQKFNLGYGWLLLTKYPVYVLLSTYYLTPLSQIAWAFIIDAISLLVARCFSRANPIKCSNQVNTQYSVSFLFTIMASVLISVLNYISQKIFLNGLILGNSHNVVTSLVAPPLPLQYLAHVPIGYVIQRVVFSERPIPQSLFLMIFLTLWNCFIPYSILFSMNWSAMFQVVGAYLSQIWIITFICWALSL
Protein: Elastase inhibitor AFUEI (Q4WZ11)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Elastase inhibitor. Non-competitive inhibitor of A.fumigatus elastase with a Ki of 1.6 nM. Inhibits the fibrinogenase and collagenase activities of A.fumigatus elastase. Inhibitor of A.flavus elastase and human leukocyte elastase, and weakly inhibits porcine pancreatic elastase. Does not inhibit elastase from P.aeruginosa or C.atrox venom.
Subcellular location: Secreted {ECO:0000269|PubMed:18566136}.
Interaction partners:
Sequence:
MKFSLACLLALAGLQAALADPATCEKEAQFVKQELIGQPYTDAVANALQSNPIRVLHPGDMITMEYIASRLNIQVNENNEIISAHCA
Protein: PAN2-PAN3 deadenylation complex catalytic subunit PAN2 (EC 3.1.13.4) (PAB1P-dependent poly(A)-specific ribonuclease) (Poly(A)-nuclease deadenylation complex subunit 2) (PAN deadenylation complex subunit 2) (P53010)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein PAB1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping by DCP1-DCP2 and subsequent 5'-3' exonucleolytic degradation by XRN1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails, trimming the tails from their synthesized length to the slightly shorter, apparently messenger-specific length found on newly exported mRNAs. PAN cooperates with protein kinase DUN1 in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15894541}.
Interaction partners:
- PAN2-PAN3 deadenylation complex subunit PAN3
- Polyadenylate-binding protein, cytoplasmic and nuclear
- CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4
- Poly
- 5'-3' exoribonuclease 1
- Proliferating cell nuclear antigen
- General negative regulator of transcription subunit 1
- mRNA-decapping enzyme subunit 1
Sequence:
MNNWQHFFNNPVDLSEHLKKPYFRFDNRDKEITAISFDEKANLIWSGDSYGCISSYDPTFQLYTRYRGHIGGNSVKDILSHRDGILSISEDSLHFANRRGVTKLNLTSIDIAAFSELNTMCYSPHSLKNNIYCGGDNTNWGIASIDLNRGCLDSLLNYSSKVKLMCSNNKVLSIGRQTGTVDLLDPTSNRTIKSFNAHSASISAMDLRDNTLVTVGKSKRFYNLYADPFVNVYDLRTMRQLPPVSFSKGTTMGSGGADFVQLHPLLPTVMIVASSSGSFDFIDLSNPTLRTQYVHPCQSIKKLCLSPNGDVLGILEADNHLDTWRRSSNNMGMFTNTPEMLAYPDYFNDITSDGPISVDDETYPLSSVGMPYYLDKLLSAWPPVVFKSEGTIPQLTGKSPLPSSGKLKSNLAVISSQNEKLSTQEFPLLRYDRTKYGMRNAIPDYVCLRDIRKQITSGLETSDIQTYTSINKYEVPPAYSRLPLTSGRFGTDNFDFTPFNNTEYSGLDPDVDNHYTNAIIQLYRFIPEMFNFVVGCLKDENFETTLLTDLGYLFDMMERSHGKICSSSNFQASLKSLTDKRQLENGEPQEHLEEYLESLCIRESIEDFNSSESIKRNMPQKFNRFLLSQLIKEEAQTVNHNITLNQCFGLETEIRTECSCDHYDTTVKLLPSLSISGINKTVIKQLNKKSNGQNILPYIEYAMKNVTQKNSICPTCGKTETITQECTVKNLPSVLSLELSLLDTEFSNIRSSKNWLTSEFYGSIIKNKAVLRSTASELKGTSHIFKYELNGYVAKITDNNNETRLVTYVKKYNPKENCFKWLMFNDYLVVEITEEEALKMTYPWKTPEIIIYCDAEELRKPFFSVDTYSINYDILFRDYFANGIRDTARREYKLLTHDEAPKSGTLVAIDAEFVSLQSELCEIDHQGIRSIIRPKRTALARISIIRGEEGELYGVPFVDDYVVNTNHIEDYLTRYSGILPGDLDPEKSTKRLVRRNVVYRKVWLLMQLGCVFVGHGLNNDFKHININVPRNQIRDTAIYFLQGKRYLSLRYLAYVLLGMNIQEGNHDSIEDAHTALILYKKYLHLKEKAIFEKVLNSVYEEGRAHNFKVPETSKG
Protein: Probable acyl-CoA dehydrogenase IBR3 (EC 1.3.99.-) (Protein INDOLE-3-BUTYRIC ACID RESPONSE 3) (Q8RWZ3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved with IBR1 and IBR10 in the peroxisomal beta-oxidation of indole-3-butyric acid (IBA) to form indole-3-acetic acid (IAA), a biologically active auxin. May be responsible for catalyzing the first step in IBA-CoA beta-oxidation. May play a role in defense response to pathogenic bacteria.
Subcellular location: Peroxisome {ECO:0000305}.
Interaction partners:
- Peroxisomal fatty acid beta-oxidation multifunctional protein AIM1
- Probable enoyl-CoA hydratase 1, peroxisomal
- Peroxisomal fatty acid beta-oxidation multifunctional protein MFP2
- 3-ketoacyl-CoA thiolase 2, peroxisomal
- Acyl-coenzyme A oxidase 3, peroxisomal
- Peroxisomal acyl-coenzyme A oxidase 1
- Acyl-coenzyme A oxidase 4, peroxisomal
- Acyl-coenzyme A oxidase 2, peroxisomal
- Putative acyl-coenzyme A oxidase 3.2, peroxisomal
- Putative peroxisomal acyl-coenzyme A oxidase 1.2
Sequence:
MGSSTGDLVTRIQSAHRFDHDALFRFAADNVSGFPTNPSQFKVSQFGHGQSNPTFLIEVGSGSSLKRYVLRKKPPGKLLQSAHAVDREFQVLRALGEHTQVPVPKVFCLCTDPAVIGTAFYIMEFMEGRIFIDPKLPNVAPERRNAIYRATAKALASLHSADVDAIGLEKYGRRGNYCKRQIDRWFKQYLASTSEGKPERNPKMFELVDWLRKNIPAEDSTGATSGLVHGDFRIDNLVFHPSEDRVIGIIDWELSTLGNQMCDVAYSCMHYIVNVQLDKEHVSEGFETTGLPEGMLSMPEFLLEYCSASGKPWPAANWKFYVAFSLFRAASIYTGVYSRWLMGNASAGERARNTGVQANELVESALGYIARENVLPEHPPSVQRDVSPSYESLVDGSGRFIPNRKVLELRQKLIKFMETHIYPMENEFSKLAQSDMRWTVHPQEEKLKEMAKREGLWNLFVPVDSAARARRELAATENKHNLSGKSFDQLFGEGLTNLEYGYLCEIMGRSVWAPQVFNCGAPDTGNMEVILRYGNKEQISEWLIPLLEGRIRSGFAMTEPQVASSDATNIECSIRRQGDSYVINGTKWWTSGAMDPRCRVLILMGKTDFNAPKHKQQSMILVDMRTPGISVKRPLTVFGFDDAPHGHAEISFENVVVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAAERGMELMAQRALSRKTFGKFIAQHGSFVSDLAKLRVELEGTRLLVLEAADHLDKFGNKKARGILAMAKVAAPNMALKVLDTAIQVHGAAGVSSDTVLAHLWATARTLRIADGPDEVHLGTIGKLELQRASKL
Protein: Odorant receptor 83a (Q9VNB3)
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. Involved in the behavioral responses to pentanol, ethyl acetate, and propyl acetate.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Odorant receptor 1a
- Odorant receptor 74a
- Odorant receptor 30a
- Odorant receptor 63a
- Odorant receptor 45b
- Odorant receptor 22c
- Odorant receptor 45a
- Odorant receptor 24a
- Odorant receptor 59a
- Odorant receptor 85c
Sequence:
MKSTFKEERIKDDSKRRDLFVFVRQTMCIAAMYPFGYYVNGSGVLAVLVRFCDLTYELFNYFVSVHIAGLYICTIYINYGQGDLDFFVNCLIQTIIYLWTIAMKLYFRRFRPGLLNTILSNINDEYETRSAVGFSFVTMAGSYRMSKLWIKTYVYCCYIGTIFWLALPIAYRDRSLPLACWYPFDYTQPGVYEVVFLLQAMGQIQVAASFASSSGLHMVLCVLISGQYDVLFCSLKNVLASSYVLMGANMTELNQLQAEQSAADVEPGQYAYSVEEETPLQELLKVGSSMDFSSAFRLSFVRCIQHHRYIVAALKKIESFYSPIWFVKIGEVTFLMCLVAFVSTKSTAANSFMRMVSLGQYLLLVLYELFIICYFADIVFQNSQRCGEALWRSPWQRHLKDVRSDYMFFMLNSRRQFQLTAGKISNLNVDRFRGTITTAFSFLTLLQKMDARE
Protein: Transposase InsI for insertion sequence element IS30A (P0CF88)
Organism: Escherichia coli (strain K12)
Function: Required for the transposition of the insertion element.
Interaction partners:
Sequence:
MRRTFTAEEKASVFELWKNGTGFSEIANILGSKPGTIFTMLRDTGGIKPHERKRAVAHLTLSEREEIRAGLSAKMSIRAIATALNRSPSTISREVQRNRGRRYYKAVDANNRANRMAKRPKPCLLDQNLPLRKLVLEKLEMKWSPEQISGWLRRTKPRQKTLRISPETIYKTLYFRSREALHHLNIQHLRRSHSLRHGRRHTRKGERGTINIVNGTPIHERSRNIDNRRSLGHWEGDLVSGTKNSHIATLVDRKSRYTIIVRLRGKDSVSVNQALTDKFLSLPSELRKSLTWDRGMELARHLEFTVSTGVKVYFCDPQSPWQRGTNENTNGLIRQYFPKKTCLAQYTQHELDLVAAQLNNRPRKTLKFKTPKEIIERGVALTD
Protein: Glucagon receptor a (Glucagon receptor isoform X1) (E7FB43)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Glucagon b
- Glucagon receptor b
- Glucagon a
- Guanine nucleotide-binding protein G
- Guanine nucleotide binding protein
- Gnb2 protein, beta polypeptide 2)/G
- Gnb1l protein, beta polypeptide 1, like), beta polypeptide 1b isoform X1), beta polypeptide 1b)
- Insulin
Sequence:
MSQVVLLLTLLSFNSCIQVSSAVSLKTMMERWMMYRDECFRNMSREAPMTGVVCNRTFDRYACWPDALPNTTVSVACPWYLPWHKEVRHGLVHVECDADGQYSKQKDASECLSRDNIQHYGRILRQFRTMYTVGYSLSLGALVLALSILVAFRKLHCMRNNIHMNLFASFILRASSILIKDALSERPDTFPVGQDITTELEVEWLVKNETAVGCRVAVVMMQYSILANSYWLLVEGIYLHSLLVVTVLTERNYLSIYLSIGWGAPLIFVLPWVIVKYLYENEECWEQNNHMEYWWIIRSPILLAVLINFFIFIHIIKILVSKLRAHQMRYSDYKFRLAKSTLTLIPLLGIHSVLFSFVTDESTSHGALPLRLTKLFIDLFFNSFQGLLVAILYCFVNKEVQSEILKKWRRWKLGRDIEEEYRHTYSQSLQIQKSGSIMVHPTNLPRLPDIATTTSRLGSPEEKQMLVSSSQNGMGIGQGCLQFTSTQQDGSTCSSITEDMVVVDRERYCRVAQGNAESNL
Protein: Mitochondrial import inner membrane translocase subunit TIM50 (Q38AF9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|RuleBase:RU365079}; Single-pass membrane protein {ECO:0000256|RuleBase:RU365079}.
Interaction partners:
Sequence:
MPRVQRVRGLSFRQEYACNDLSCAGCRGSPKSSATQALIAPKDKRLADRPTIVLDLDETLVYAREGPLYVRPGLEELLQFLDENCETVLWTAGMKHYAEAVVRHIDRHNAVHHMIYRSSDWFRGGSTAKDLSLLGRDVATTIVFENTPDSIRGFEQNGVLVADYVGGELEDHTLSAILGLLRDFVERRRHDTNLTVPEFIRSSHRLEQREVPTDDGDMMLCYCLIVREGMYGYDKTNEVDGGMEPLHKRRHNKLVEAKRRWNLLVR
Protein: Pentatricopeptide repeat-containing protein At1g80270, mitochondrial (Q9C977)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- Probable lipid-A-disaccharide synthase, mitochondrial
- Pentatricopeptide repeat-containing protein At4g35850
- Small ribosomal subunit protein uS3m
- Pentatricopeptide repeat-containing protein At4g21880
- Pentatricopeptide repeat-containing protein At3g18020
- GrpE protein homolog 2
- Mitochondrial outer membrane protein porin 4
- Pentatricopeptide repeat-containing protein At1g08070, chloroplastic
- GrpE protein homolog 1
Sequence:
MFALSKVLRRTQRLRLGACSAVFSKDIQLGGERSFDSNSIASTKREAVPRFYEISSLSNRALSSSAGTKSDQEEDDLEDGFSELEGSKSGQGSTSSDEDEGKLSADEEEEEELDLIETDVSRKTVEKKQSELFKTIVSAPGLSIGSALDKWVEEGNEITRVEIAKAMLQLRRRRMYGRALQMSEWLEANKKIEMTERDYASRLDLTVKIRGLEKGEACMQKIPKSFKGEVLYRTLLANCVAAGNVKKSELVFNKMKDLGFPLSGFTCDQMLLLHKRIDRKKIADVLLLMEKENIKPSLLTYKILIDVKGATNDISGMEQILETMKDEGVELDFQTQALTARHYSGAGLKDKAEKVLKEMEGESLEANRRAFKDLLSIYASLGREDEVKRIWKICESKPYFEESLAAIQAFGKLNKVQEAEAIFEKIVKMDRRASSSTYSVLLRVYVDHKMLSKGKDLVKRMAESGCRIEATTWDALIKLYVEAGEVEKADSLLDKASKQSHTKLMMNSFMYIMDEYSKRGDVHNTEKIFLKMREAGYTSRLRQFQALMQAYINAKSPAYGMRDRLKADNIFPNKSMAAQLAQGDPFKKTAISDILD
Protein: Alpha-thujene synthase, chloroplastic (EC 4.2.3.-) (Terpene synthase 2) (LcTPS2) (G0Y7D2)
Organism: Litsea cubeba (Aromatic litsea) (Laurus cubeba)
Function: Monoterpene synthase (TPS) involved in the biosynthesis of monoterpene natural products used by traditional Chinese medicine to treat headache, inflammation and intoxication (Ref.1). Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) into alpha-thujene (Ref.1).
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MALQLLTPSFSFQHSPSPHKLTTLRYTHHRIRCTASAPSYSDLVRRRSANYKPSKWDSNFVETLESDYKKENHEMYIEKLMGDVKHLMKEVVNPIEKMELVDTIQRLGLGYLFNKEIKEVLNTITTSKATLKTKKDLHAVALQFRLLRQHGYEVSPDAFHEFKDEKGGFKESLCMDIKGMLCLYEASHLSFQGEVVLDEAREFTSTHLKAIGGNIDPVLLKKVRHSLEMPLHWRMLRLEARWYIETYDEEDRKNPSLAELAKHDFNSVQTIYQRSLKRMSRWWRDLGLGERLEFSRDRLVECFFWTTGVIFDPQFERCRGVLTKVNQLVSTIDDVYDVYGSLEELELFTDAVDRWDIRAMEQLPEYMKICYLALYNTTNDIAYEALKEEGLDVIPYLKKVWTDLCKSYIVEARWYSNGYKPTLEEYLENAWTSIAGPVALVHAYFSFGQKMPFEALNYSNTSSLIKWSSMIFRLCDDLATSSDEVARGDVPKSIQCYMYEAGVSESVARDHIKYLIDEAWKKMNECLVYNTPFLQPLINAGLNLARMAHCMYERGDGHGFSNELDKKRVLLLLAEPFKFM
Protein: Large ribosomal subunit protein bL28m (39S ribosomal protein L28, mitochondrial) (L28mt) (MRP-L28) (Q9VMX0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q13084}.
Interaction partners:
- Large ribosomal subunit protein uL4m
- Small ribosomal subunit protein mS26
- Large ribosomal subunit protein mL66
- Large ribosomal subunit protein mL64
- Large ribosomal subunit protein bL9m
- GM03767p
- Large ribosomal subunit protein mL41
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein uL16m
- Large ribosomal subunit protein mL40
Sequence:
MAHATPQGVKLLNGWKRPGRFDKGLGAQLPEAYRKFWREWKLTTPAAVHYIPKEQQWERDEVTHAIKPVQNIPLPLIDTPESHRGIWGGEAVIKGFQKREQTKRRVPHFWVPNLRRSVVHSHVLDCYMSVVVTERTLEQIHECHGFDHYLLKNRACDLRSALALKLKREVLQALQNGVPALADEPERQQEVLKEYRRYLEPYTPEEIDWYGHTYLEAIRKLQKQLREAEKVVPHKLEFRGKLIEQLRQAGISEAGKLEKPDALAAESSVEHKDSDIEALTKLESSPSSSWLSKINPFGKKET
Protein: Neutrophil collagenase (EC 3.4.24.34) (Collagenase 2) (Matrix metalloproteinase-8) (MMP-8) (O70138)
Organism: Mus musculus (Mouse)
Function: Can degrade fibrillar type I, II, and III collagens. May play a role in the degradation of collagen fibers during uterine involution.
Subcellular location: Cytoplasmic granule. Secreted, extracellular space, extracellular matrix. Note=Stored in intracellular granules and released during inflammatory conditions.
Interaction partners:
- Metalloproteinase inhibitor 1
- Metalloproteinase inhibitor 2
- Neutrophil elastase
- Matrilysin
- Matrix metalloproteinase-9
- Alpha-2-macroglobulin-P
- Lactotransferrin
- Myeloperoxidase
- Metalloproteinase inhibitor 4
- Metalloproteinase inhibitor 3
Sequence:
MFRLKTLPLLIFLHTQLANAFPVPEHLEEKNIKTAENYLRKFYNLPSNQFRSSRNATMVAEKLKEMQRFFSLAETGKLDAATMGIMEMPRCGVPDSGDFLLTPGSPKWTHTNLTYRIINHTPQLSRAEVKTAIEKAFHVWSVASPLTFTEILQGEADINIAFVSRDHGDNSPFDGPNGILAHAFQPGQGIGGDAHFDSEETWTQDSKNYNLFLVAAHEFGHSLGLSHSTDPGALMYPNYAYREPSTYSLPQDDINGIQTIYGPSDNPIQPTGPSTPKACDPHLRFDATTTLRGEIYFFKDKYFWRRHPQLRTVDLNFISLFWPFLPNGLQAAYEDFDRDLVFLFKGRQYWALSGYDLQQGYPRDISNYGFPRSVQAIDAAVSYNGKTYFFINNQCWRYDNQRRSMDPGYPKSIPSMFPGVNCRVDAVFLQDSFFLFFSGPQYFAFNFVSHRVTRVARSNLWLNCS
Protein: Heparin and heparin-sulfate lyase (Heparin lyase) (EC 4.2.2.7) (Heparin-sulfate lyase) (EC 4.2.2.8) (Heparinase II) (HepII) (C6XZB6)
Organism: Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3)
Function: Cleaves both heparin and heparan sulfate glycosaminoglycans through a beta-elimination mechanism. Cleaves heparin at alpha-D-GlcNp2S6S(1->4) alpha-L-IdoAp2S and heparan sulfate at alpha-D-GlcNp2Ac(or 2S)6OH(1->4)beta-D-GlcAp.
Subcellular location: Periplasm {ECO:0000269|PubMed:8702264}.
Interaction partners:
- Methyltransferase type 12
Sequence:
MKRQLYLYVIFVVVELMVFTTKGYSQTKADVVWKDVDGVSMPIPPKTHPRLYLREQQVPDLKNRMNDPKLKKVWADMIKMQEDWKPADIPEVKDFRFYFNQKGLTVRVELMALNYLMTKDPKVGREAITSIIDTLETATFKPAGDISRGIGLFMVTGAIVYDWCYDQLKPEEKTRFVKAFVRLAKMLECGYPPVKDKSIVGHASEWMIMRDLLSVGIAIYDEFPEMYNLAAGRFFKEHLVARNWFYPSHNYHQGMSYLNVRFTNDLFALWILDRMGAGNVFNPGQQFILYDAIYKRRPDGQILAGGDVDYSRKKPKYYTMPALLAGSYYKDEYLNYEFLKDPNVEPHCKLFEFLWRDTQLGSRKPDDLPLSRYSGSPFGWMIARTGWGPESVIAEMKVNEYSFLNHQHQDAGAFQIYYKGPLAIDAGSYTGSSGGYNSPHNKNFFKRTIAHNSLLIYDPKETFSSSGYGGSDHTDFAANDGGQRLPGKGWIAPRDLKEMLAGDFRTGKILAQGFGPDNQTPDYTYLKGDITAAYSAKVKEVKRSFLFLNLKDAKVPAAMIVFDKVVASNPDFKKFWLLHSIEQPEIKGNQITIKRTKNGDSGMLVNTALLPDAANSNITSIGGKGKDFWVFGTNYTNDPKPGTDEALERGEWRVEITPKKAAAEDYYLNVIQIADNTQQKLHEVKRIDGDKVVGVQLADRIVTFSKTSETVDRPFGFSVVGKGTFKFVMTDLLPGTWQVLKDGKILYPALSAKGDDGALYFEGTEGTYRFLR