wanglab/gogpt-training-data huggingface dataset:
Protein: Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (EC 3.1.3.16) (EC 3.1.3.48) (EC 3.1.3.67) (Inositol polyphosphate 3-phosphatase) (Q9Y0B6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}. Synapse {ECO:0000256|ARBA:ARBA00034103}.
Interaction partners:
Sequence:
MANTISLMSNVIRNVVSKKRIRYKEKGYDLDLTYINDNIIAMGYPAPDKLEGLFRNRLEDVFKLLEENHAQHYKIYNLCSERSYDVAKFRGRVAVYPFDDHNPPTIELIQRFCSDVDMWLKEDSSNVVAVHCKAGKGRTGTMICAYLVFSGIKKSADEALAWYDEKRTKDRKGVTIPSQRRYVQYFSKLVCSSVPYSKVSLNVCEIRFSESSCVQNLGMVECSISVLHDSATENAKPDRLKTLPIDFQKSFVLTIKPSIPVSGDVKFELTKKSPDKIICHFWLNTFFVRNYSPCESDGTVNKYIHTLSKSEIDDVHKDSEHKRFSEEFKISIVFEAENFSNDVQAEASEKERNENVLNFERSDYDSLSPNCYAEKKVLTAIVNDNTTKSQTIETLDHKDIVVNQHTCNQCLLRTYNSW
Protein: PE_PGRS family protein (Q7D4U2)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MSFVVTVPEAVAAAAGDLAAIGSTLREATAAAAGPTTGLAAAAADDVSIAVSQLFGRYGQEFQTVSNQLAAFHTEFVRTLNRGAAAYLNTESANGGQLFGQIEAGQRAVSAAAAAAPGGAYGQLVANTATNLESLYGAWSANPFPFLRQIIANQQVYWQQIAAALANAVQNFPALVANLPAAIDAAVQQFLAFNAAYYIQQIISSQIGFAQLFATTVGQGVTSVIAGWPNLAAELQLAFQQLLVGDYNAAVANLGKAMTNLLVTGFDTSDVTIGTMGTTISVTAKPKLLGPLGDLFTIMTIPAQEAQYFTNLMPPSILRDMSQNFTNVLTTLSNPNIQAVASFDIATTAGTLSTFFGVPLVLTYATLGAPFASLNAIATSAETIEQALLAGNYLGAVGALIDAPAHALDGFLNSATVLDTPILVPTGLPSPLPPTVGITLHLPFDGILVPPHPVTATISFPGAPVPIPGFPTTVTVFGTPFMGMAPLLINYIPQQLALAIKPAA
Protein: Adenylate kinase 8 (AK 8) (EC 2.7.4.3) (EC 2.7.4.6) (ATP-AMP transphosphorylase 8) (Q96MA6)
Organism: Homo sapiens (Human)
Function: Nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. Has highest activity toward AMP, and weaker activity toward dAMP, CMP and dCMP. Also displays broad nucleoside diphosphate kinase activity.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:21080915}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:33139725}. Note=Located in the proximal region of respiratory cilia. {ECO:0000269|PubMed:33139725}.
Interaction partners:
- Adenylosuccinate lyase
- Adenine phosphoribosyltransferase
- Adenosine kinase
- Cancer-related nucleoside-triphosphatase
- Deoxycytidine kinase
- Pyruvate kinase PKM
- Pyruvate kinase PKLR
- Ectonucleoside triphosphate diphosphohydrolase 2
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
Sequence:
MDATIAPHRIPPEMPQYGEENHIFELMQNMLEQLLIHQPEDPIPFMIQHLHRDNDNVPRIVILGPPASGKTTIAMWLCKHLNSSLLTLENLILNEFSYTATEARRLYLQRKTVPSALLVQLIQERLAEEDCIKQGWILDGIPETREQALRIQTLGITPRHVIVLSAPDTVLIERNLGKRIDPQTGEIYHTTFDWPPESEIQNRLMVPEDISELETAQKLLEYHRNIVRVIPSYPKILKVISADQPCVDVFYQALTYVQSNHRTNAPFTPRVLLLGPVGSGKSLQAALLAQKYRLVNVCCGQLLKEAVADRTTFGELIQPFFEKEMAVPDSLLMKVLSQRLDQQDCIQKGWVLHGVPRDLDQAHLLNRLGYNPNRVFFLNVPFDSIMERLTLRRIDPVTGERYHLMYKPPPTMEIQARLLQNPKDAEEQVKLKMDLFYRNSADLEQLYGSAITLNGDQDPYTVFEYIESGIINPLPKKIP
Protein: Nodulin homeobox (NDX1 homeobox protein homolog) (AtNDX1) (F4JI44)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Regulates COOLAIR, a set of antisense transcripts originating from the 3' end of FLOWERING LOCUS C (FLC). Associates with single-stranded DNA that is part of an RNA-DNA hybrid, or R-loop, that covers the COOLAIR promoter. R-loop stabilization mediated by NDX inhibits COOLAIR transcription, which in turn modifies FLC expression.
Subcellular location: Nucleus {ECO:0000269|PubMed:23641115}. Nucleus, nucleolus {ECO:0000269|PubMed:23641115}.
Interaction partners:
- Homeobox-DDT domain protein RLT3
- E2F/DP family winged-helix DNA-binding domain-containing protein
- Protein NEOXANTHIN-DEFICIENT 1
- Ac-like transposase
- HAT family dimerization domain-containing protein
- Cleavage stimulation factor subunit 77
- Protein HUA2-LIKE 2
- Homeobox-leucine zipper protein ATHB-8
Sequence:
MVRLLQPKHMVQAVNALHWRNSVEFHKLLKDNGDFSICFNSEQVLPQKISVEKMVKMLPRHLIAVVMTPNKDGKSRYILCGIRLLQTLCDLTPRNAKLEQVLLDDVKLSAQMIDLVILVIIALGRNRKESCNSNKESLLEATLVASCLHLFHGFISPNSQDLVLVLLAHPRVDVFIDSAFGAVLNVVISLKAKLLYRQTDSPKKLGASSVEEVNFHCQQAEAALQFLHSLCQHKPFRERVAKNKELCGKGGVLRLAQSILSLTITPEFVGATVTIASTSRMKAKVLSILQHLFEAESVSFLDEVANAGNLHLAKTVASEVLKLLRLGLSKASMATASPDYPMGFVLLNAMRLADVLTDDSNFRSFFTEHFSMVLSAVFCLSHGDFLSMLCSSDLSSREDDANVDYDLFKSAGWILSVFSSSGQSVTPQFKLSLQNNLTMSSYAHQRTSLFIKMIANLHCFVPNVCQEQDRNRFIQNVMSGLRKDPSSILIKMLPGSSYTPVAQRGTGVCRNLGSLLRHAESLIPSSLNEEDFLLLRVFCDQLQPLIHSEFEESQVQVKVKKLFALLYIGFTILWLICLVTLIQDIEGRGGNLSGKLKELLNLNNEEASEDCDVRVEGVMTKQGVNEEIDTVERLKESDADASNLETSGSDTSSNRGKGLVEEGELVQNMSKRFKGSASGEVKEDEKSETFLVFEKQKKKRKRSIMNADQMGMIEKALAEEPDLQRNSASRQLWADKISQKGSEVITSSQLKNWLNNRKAKLARANKQTGPAHDNNSSGDLPESPGDENTWQQKPSTPIKDQTVTETPKTGENLMRTSSSSEEGIKQGQQVRLMDERGDEIGKGTVLRTDGEWNGLSLETRQICVVDVMELSESYDGSKKMIPYGSDDVGRTFTEANSRFGVMRVAWDVNKLQY
Protein: P2Y purinoceptor 4 (P2Y4) (O35811)
Organism: Rattus norvegicus (Rat)
Function: Receptor for ATP and UTP coupled to G-proteins that activate a phosphatidylinositol-calcium second messenger system. Not activated by ADP or UDP.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- P2X purinoceptor 1
- P2X purinoceptor 2
- P2X purinoceptor 6
- P2X purinoceptor 3
- P2X purinoceptor 7
- P2X purinoceptor 4
- Guanine nucleotide-binding protein G
Sequence:
MTSAESLLFTSLGPSPSSGDGDCRFNEEFKFILLPMSYAVVFVLGLALNAPTLWLFLFRLRPWDATATYMFHLALSDTLYVLSLPTLVYYYAARNHWPFGTGLCKFVRFLFYWNLYCSVLFLTCISVHRYLGICHPLRAIRWGRPRFASLLCLGVWLVVAGCLVPNLFFVTTNANGTTILCHDTTLPEEFDHYVYFSSAVMVLLFGLPFLITLVCYGLMARRLYRPLPGAGQSSSRLRSLRTIAVVLTVFAVCFVPFHITRTIYYQARLLQADCHVLNIVNVVYKVTRPLASANSCLDPVLYLFTGDKYRNQLQQLCRGSKPKPRTAASSLALVTLHEESISRWADTHQDSTFSAYEGDRL
Protein: Glycine-rich protein (Q9M1A4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Autophagy-related protein 8a
- Arabidiol synthase
Sequence:
MSSTQANLCRPSLFCARTTQTRHVSSAPFMSSLRFDYRPLPKLAIRASASSSMSSQFSPLQNHRCRNQRQGPVVCLLGGKDKSNGSNELSSTWEAIEKAMGKKSVEDMLREQIQKKDTGGIPPRGRGGGGGGRNGGNNGSGGSSGEDGGLASFGDETLQVVLATLGFIFLYFYIINGEELFRLARDYIRYLIGRPKSVRLTRVMEGWSRFFEKMSRKKVYNEYWLKIKRSSTSLPGLVTRANTNAS
Protein: Trichohyalin (Q07283)
Organism: Homo sapiens (Human)
Function: Intermediate filament-associated protein that associates in regular arrays with keratin intermediate filaments (KIF) of the inner root sheath cells of the hair follicle and the granular layer of the epidermis. It later becomes cross-linked to KIF by isodipeptide bonds. It may serve as scaffold protein, together with involucrin, in the organization of the cell envelope or even anchor the cell envelope to the KIF network. It may be involved in its own calcium-dependent postsynthetic processing during terminal differentiation.
Interaction partners:
- Loricrin
- Involucrin
- Protein-arginine deiminase type-3
- Protein S100-A10
- Cornifin-A
- Small proline-rich protein 3
- Filaggrin
- Repetin
- Cornifin-B
- Protein S100-A6
Sequence:
MSPLLRSICDITEIFNQYVSHDCDGAALTKKDLKNLLEREFGAVLRRPHDPKTVDLILELLDLDSNGRVDFNEFLLFIFKVAQACYYALGQATGLDEEKRARCDGKESLLQDRRQEEDQRRFEPRDRQLEEEPGQRRRQKRQEQERELAEGEEQSEKQERLEQRDRQRRDEELWRQRQEWQEREERRAEEEQLQSCKGHETEEFPDEEQLRRRELLELRRKGREEKQQQRRERQDRVFQEEEEKEWRKRETVLRKEEEKLQEEEPQRQRELQEEEEQLRKLERQELRRERQEEEQQQQRLRREQQLRRKQEEERREQQEERREQQERREQQEERREQQLRREQEERREQQLRREQEEERREQQLRREQEEERREQQLRREQQLRREQQLRREQQLRREQQLRREQQLRREQQLRREQQLRREQQLRREQEEERHEQKHEQERREQRLKREQEERRDWLKREEETERHEQERRKQQLKRDQEEERRERWLKLEEEERREQQERREQQLRREQEERREQRLKRQEEEERLQQRLRSEQQLRREQEERREQLLKREEEKRLEQERREQRLKREQEERRDQLLKREEERRQQRLKREQEERLEQRLKREEVERLEQEERREQRLKREEPEEERRQQLLKSEEQEERRQQQLRREQQERREQRLKREEEEERLEQRLKREHEEERREQELAEEEQEQARERIKSRIPKWQWQLESEADARQSKVYSRPRKQEGQRRRQEQEEKRRRRESELQWQEEERAHRQQQEEEQRRDFTWQWQAEEKSERGRQRLSARPPLREQRERQLRAEERQQREQRFLPEEEEKEQRRRQRREREKELQFLEEEEQLQRRERAQQLQEEEDGLQEDQERRRSQEQRRDQKWRWQLEEERKRRRHTLYAKPALQEQLRKEQQLLQEEEEELQREEREKRRRQEQERQYREEEQLQQEEEQLLREEREKRRRQERERQYRKDKKLQQKEEQLLGEEPEKRRRQEREKKYREEEELQQEEEQLLREEREKRRRQEWERQYRKKDELQQEEEQLLREEREKRRLQERERQYREEEELQQEEEQLLGEERETRRRQELERQYRKEEELQQEEEQLLREEPEKRRRQERERQCREEEELQQEEEQLLREEREKRRRQELERQYREEEEVQQEEEQLLREEPEKRRRQELERQYREEEELQQEEEQLLREEQEKRRQERERQYREEEELQRQKRKQRYRDEDQRSDLKWQWEPEKENAVRDNKVYCKGRENEQFRQLEDSQLRDRQSQQDLQHLLGEQQERDREQERRRWQQRDRHFPEEEQLEREEQKEAKRRDRKSQEEKQLLREEREEKRRRQETDRKFREEEQLLQEREEQPLRRQERDRKFREEELRHQEQGRKFLEEEQRLRRQERERKFLKEEQQLRCQEREQQLRQDRDRKFREEEQQLSRQERDRKFREEEQQVRRQERERKFLEEEQQLRQERHRKFREEEQLLQEREEQQLHRQERDRKFLEEEQQLRRQERDRKFREQELRSQEPERKFLEEEQQLHRQQRQRKFLQEEQQLRRQERGQQRRQDRDRKFREEEQLRQEREEQQLSRQERDRKFRLEEQKVRRQEQERKFMEDEQQLRRQEGQQQLRQERDRKFREDEQLLQEREEQQLHRQERDRKFLEEEPQLRRQEREQQLRHDRDRKFREEEQLLQEGEEQQLRRQERDRKFREEEQQLRRQERERKFLQEEQQLRRQELERKFREEEQLRQETEQEQLRRQERYRKILEEEQLRPEREEQQLRRQERDRKFREEEQLRQEREEQQLRSQESDRKFREEEQLRQEREEQQLRPQQRDGKYRWEEEQLQLEEQEQRLRQERDRQYRAEEQFATQEKSRREEQELWQEEEQKRRQERERKLREEHIRRQQKEEQRHRQVGEIKSQEGKGHGRLLEPGTHQFASVPVRSSPLYEYIQEQRSQYRP
Protein: SNF7 family protein Fti1/Did2, putative (AFU_orthologue AFUA_3G04060) (Q5AQN4)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Vta1 C-terminal domain-containing protein
- vesicle-fusing ATPase
- SNF7 family protein
- DUF292 domian protein
- Vacuolar-sorting protein snf7
- SNF7 family protein
- SNF7 family protein
- SNF7 family protein
- Vacuolar sorting protein SNF7 family protein, putative
- Vacuolar protein sorting-associated protein 28
Sequence:
MVRKDPIFEARTNVKLHSNRLKKEAARAEATFKSEKAKADKAMKNREFQIARIHASSAVREKRRQVTLKAEAARADVIINELKAAQSTRDTSRTLALASRGLDAASKSVNLETLVSHANNFLARSEDFKIASNAIEDVAQGVSMQEYGAEGEADVDRLMEQLADDAGVDLRLALEQDSAPKEDVKEQTKVDADVEDGLGARLRALRAAN
Protein: Low molecular weight phosphotyrosine protein phosphatase 2 (EC 3.1.3.48) (Low molecular weight cytosolic acid phosphatase 2) (EC 3.1.3.2) (PTPase 2) (P82891)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the dephosphorylation of tyrosine phosphorylated proteins and low-MW aryl phosphates. Can contribute to the regulation of a variety of developmental processes.
Subcellular location: Cytoplasm.
Interaction partners:
- Arginine phosphatase
- Thiamine pyrophosphokinase 1
- Low molecular weight phosphotyrosine protein phosphatase 1
- FAD synthase
- FAD synthase
- acid phosphatase
- GH19849p
- IP06402p
- Putative riboflavin kinase
- Uncharacterized protein, isoform B
Sequence:
MGKRSQKSSVLMVCVGNLCRSPIAEAVMRDLVARAGLQGEWHVESAGIEDWHSGHQPDERALNVLARHNIEYNGKARVLAPEDFLEFDYIFAMDLSNLAALRRMAPKGTTAKLLILGNFGLKPDERIIEDPYYDIGEASFEEIYRQCSIACRNFLKQARLKQIM
Protein: GTP cyclohydrolase-2 (EC 3.5.4.25) (GTP cyclohydrolase II) (P38066)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.
Interaction partners:
- Riboflavin synthase
- 2,5-diamino-6-ribosylamino-4
- 6,7-dimethyl-8-ribityllumazine synthase
- 3,4-dihydroxy-2-butanone 4-phosphate synthase
- GTP cyclohydrolase 1
- Bifunctional protein RIB2
- Riboflavin kinase
- Nucleoside diphosphate kinase
- Inosine triphosphate pyrophosphatase
- Probable metabolite transport protein YBR241C
Sequence:
MTIDNYDNSKQDSSKYEVSGTGDGRNGDGGLPLVQCVARARIPTTQGPDIFLHLYSNNRDNKEHLAIVFGEDIRSRSLFRRRQCETQQDRMIRGAYIGKLYPGRTVADEDDRLGLALEFDDSTGELLASKATTWDAHNDTLVRIHSECYTGENAWSARCDCGEQFDRAGRLIACDHEPTSNIKGGNGHGVIVYLRQEGRGIGLGEKLKAYNLQDLGADTVQANLMLKHPVDARDFSLGKAILLDLGIGNVRLLTNNPEKIKQVDHAPYLKCVERVPMVPIHWTNSSEGIDSKEIEGYLRTKIERMGHLLTEPLKLHTNPQPTETSEAQNQNRMNSALSSTSTLAI
Protein: Small ribosomal subunit protein eS28 (40S ribosomal protein S28) (Q9VAB9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- 40S ribosomal protein S24
- Small ribosomal subunit protein eS21
- Small ribosomal subunit protein eS26
- Small ribosomal subunit protein eS6
- Ribosomal protein S30, isoform A
- Small ribosomal subunit protein eS7
- Small ribosomal subunit protein uS12
- Ubiquitin-ribosomal protein eS31 fusion protein
- Small ribosomal subunit protein eS4
- Small ribosomal subunit protein uS15
Sequence:
MDKPQYARVVEILGRTGSQGQCTQVRVEFLGDQSRQIIRNVKGPVRVGDILSLLETEREARRLR
Protein: Phospholipid scramblase (Q7JKP1)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MQQPVINQQPGYNPQGMNPVQQFEMHQQQHQQAITTQPGVFVQPAPGSVWMPMPPAIQGVPTGLEYLTYLDTIMVHQIKELIEIVTDWETKNKYVLKNANGEQCYYAFEESGCCERQCCGPQRGFVMHIVDNFKREVLTIKREFKCCGGGCCGCLACIGCCQQECIIETPSMGVLGIIRQRCGCMSSNYDIMDGDGNVIFQIDGPCCCMLCGCQDKEFPIKTANNGTVVGAITKKWGGCFREAFTDADTFAVNFPGDLDVKLKGVLIGATFLIDFMEFEQQSQNRNNGV
Protein: Sestrin-1 (EC 1.11.1.-) (p53-regulated protein PA26) (Q9Y6P5)
Organism: Homo sapiens (Human)
Function: Functions as an intracellular leucine sensor that negatively regulates the TORC1 signaling pathway through the GATOR complex. In absence of leucine, binds the GATOR subcomplex GATOR2 and prevents TORC1 signaling. Binding of leucine to SESN2 disrupts its interaction with GATOR2 thereby activating the TORC1 signaling pathway. This stress-inducible metabolic regulator may also play a role in protection against oxidative and genotoxic stresses (By similarity). May positively regulate the transcription by NFE2L2 of genes involved in the response to oxidative stress by facilitating the SQSTM1-mediated autophagic degradation of KEAP1. Moreover, may prevent the accumulation of reactive oxygen species (ROS) through the alkylhydroperoxide reductase activity born by the N-terminal domain of the protein (By similarity). Was originally reported to contribute to oxidative stress resistance by reducing PRDX1. However, this could not be confirmed (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:9926927}. Cytoplasm {ECO:0000269|PubMed:15105503}.
Interaction partners:
- Sestrin-2
- Sestrin-3
- GATOR2 complex protein WDR24
- Tuberin
- Cellular tumor antigen p53
- E3 ubiquitin-protein ligase RBX1
- Kelch-like ECH-associated protein 1
- 5'-AMP-activated protein kinase subunit beta-1
- Voltage-dependent calcium channel subunit alpha-2/delta-2
- GATOR2 complex protein WDR59
Sequence:
MRLAAAANEAYTAPLAVSGLLGCKQCGGGRDQDEELGIRIPRPLGQGPSRFIPEKEILQVGSEDAQMHALFADSFAALGRLDNITLVMVFHPQYLESFLKTQHYLLQMDGPLPLHYRHYIGIMAAARHQCSYLVNLHVNDFLHVGGDPKWLNGLENAPQKLQNLGELNKVLAHRPWLITKEHIEGLLKAEEHSWSLAELVHAVVLLTHYHSLASFTFGCGISPEIHCDGGHTFRPPSVSNYCICDITNGNHSVDEMPVNSAENVSVSDSFFEVEALMEKMRQLQECRDEEEASQEEMASRFEIEKRESMFVFSSDDEEVTPARAVSRHFEDTSYGYKDFSRHGMHVPTFRVQDYCWEDHGYSLVNRLYPDVGQLIDEKFHIAYNLTYNTMAMHKDVDTSMLRRAIWNYIHCMFGIRYDDYDYGEINQLLDRSFKVYIKTVVCTPEKVTKRMYDSFWRQFKHSEKVHVNLLLIEARMQAELLYALRAITRYMT
Protein: Cyclic dof factor 1 (Dof zinc finger protein DOF5.5) (AtDOF5.5) (Q8W1E3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that binds specifically to a 5'-AA[AG]G-3' consensus core sequence. A flanking TGT sequence contributes to the specificity of binding. Regulates a photoperiodic flowering response. Transcriptional repressor of 'CONSTANS' expression. The DNA-binding ability is not modulated by 'GIGANTEA' but the stability of CDF1 is controlled by the proteasome-dependent pathway. Ubiquitinated by the SCF(ADO3) E3 ubiquitin ligase complex. Binds to the FT promoter in the morning.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00071, ECO:0000269|PubMed:16002617}.
Interaction partners:
- Adagio protein 3
- Protein GIGANTEA
- Adagio protein 2
- Corepressor
- Protein CCA1
- Two-component response regulator-like APRR9
- Protein LHY
- Two-component response regulator-like APRR1
- Two-component response regulator-like APRR5
- Two-component response regulator-like APRR7
Sequence:
MLETKDPAIKLFGMKIPFPTVLEVADEEEEKNQNKTLTDQSEKDKTLKKPTKILPCPRCNSMETKFCYYNNYNVNQPRHFCKACQRYWTSGGTMRSVPIGAGRRKNKNNSPTSHYHHVTISETNGPVLSFSLGDDQKVSSNRFGNQKLVARIENNDERSNNNTSNGLNCFPGVSWPYTWNPAFYPVYPYWSMPVLSSPVSSSPTSTLGKHSRDEDETVKQKQRNGSVLVPKTLRIDDPNEAAKSSIWTTLGIKNEVMFNGFGSKKEVKLSNKEETETSLVLCANPAALSRSINFHEQM
Protein: Adenylyl-sulfate kinase 4, chloroplastic (EC 2.7.1.25) (ATP adenosine-5'-phosphosulfate 3'-phosphotransferase 4) (Adenosine-5'-phosphosulfate kinase 4) (APS kinase 4) (Q84JF0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the phosphorylation of adenosine 5'-phosphosulfate to 3'-phosphoadenylyl sulfate, which is the activated sulfate form for sulfation reactions. Essential for plant reproduction and viability.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:19304933}.
Interaction partners:
- ATP sulfurylase 2
- ATP sulfurylase 1, chloroplastic
- ATP sulfurylase 4, chloroplastic
- ATP-sulfurylase 3, chloroplastic
- 5'-adenylylsulfate reductase 2, chloroplastic
- 5'-adenylylsulfate reductase 1, chloroplastic
- 5'-adenylylsulfate reductase 3, chloroplastic
- Assimilatory sulfite reductase
- FAD synthase
- Adenylyl-sulfate kinase 2, chloroplastic
Sequence:
MDVAAMARCVGRCYVSPAFGESESHRLSERRFLKLSSSTNSDPAGSKSLKLRGKIHRRMSYFRPIMAKDESISSRSGETKQINGKQKNIVWHDCPVTKSDRQELIKQKGCVIWITGLSGSGKSSLACALSRALHNRGKLSYILDGDNVRHGLNSDLSFEADDRAENIRRVGEVAKLFADSGIICIASLISPYRIERAACRALLPQGDFIEVFMDVPLHVCEARDPKGLYKRARAGKIKGFTGVDDPYEAPLDCEIVIQNSRDKGLSSSSSSSSSPSSSSSSLCEMADIVVSYLDQNGYLKKHSTKSRNCM
Protein: Lysophospholipid acyltransferase 1 (LPLAT 1) (EC 2.3.1.-) (1-acylglycerophosphocholine O-acyltransferase) (EC 2.3.1.23) (1-acylglycerophosphoethanolamine O-acyltransferase MBOAT1) (EC 2.3.1.n7) (1-acylglycerophosphoserine O-acyltransferase MBOAT1) (EC 2.3.1.n6) (Lysophosphatidylethanolamine acyltransferase 1) (LPE acyltransferase 1) (LPEAT1) (Lyso-PE acyltransferase) (Lysophosphatidylserine acyltransferase) (LPSAT) (Lyso-PS acyltransferase) (Membrane-bound O-acyltransferase domain-containing protein 1) (O-acyltransferase domain-containing protein 1) (Q8BH98)
Organism: Mus musculus (Mouse)
Function: Acyltransferase which catalyzes the transfert of an acyl group from an acyl-CoA towards a lysophospholipid producing a phospholipid and participates in the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle. Acts on lysophosphatidylserine (1-acyl-2-hydroxy-sn-glycero-3-phospho-L-serine or LPS) and lysophosphatidylethanolamine (1-acyl-sn-glycero-3-phosphoethanolamine or LPE), and to a lesser extend lysophosphatidylcholine. Prefers oleoyl-CoA as the acyl donor and 1-oleoyl-LPE as acceptor. May play a role in neurite outgrowth during neuronal differentiation.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Endoplasmic reticulum {ECO:0000269|PubMed:18287005}.
Interaction partners:
- Lysocardiolipin acyltransferase 1
- 1-acyl-sn-glycerol-3-phosphate acyltransferase delta
- Lysophospholipid acyltransferase LPCAT4
- Choline/ethanolaminephosphotransferase 1
- 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha
- Phospholipase A1 member A
- Ethanolaminephosphotransferase 1
- Phospholipase B1, membrane-associated
- 1-acyl-sn-glycerol-3-phosphate acyltransferase beta
- 1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon
Sequence:
MAARPPASLSYRTTGSTCLHPLSQLLGIPLDQVNFVACQLFALSAAFWFRIYLHPGKASPEVRHTLATILGIYFVVFCFGWYAVHLFVLVLMCYGVMVTASVSNIHRYSFFVAMGYLTICHISRIYIFHYGILTTDFSGPLMIVTQKITTLAFQVHDGLGRKAEDLSAEQHRLAVKAKPSLLEYLSYHLNFMSVIAGPCNNFKDYVAFIEGRHIHMKLLEVNWTQRGFQSLPEPSPMGAVIQKLCVTLMSLLLFLTLSKSFPVTFLIDDWFVHKANFLSRLWYLYVVMQAAKPKYYFAWTLADAVHNAAGFGFNGMDTDGKSRWDLLSNLNIWKIETATSFKMYLENWNIQTSTWLKCVCYERVPWYPTVLTFLLSALWHGVYPGYYFTFLTGVPVTLAARAVRNNYRHHFLSSKARKIAYDVVTWAVTQLAVSYTAAPFVMLAVEPTISLYKSVFFFLHIICLLIILFLPIKPHQPQRQSRSPNSVKKKAD
Protein: Taste receptor type 2 member 40 (T2R40) (Taste receptor type 2 member 1) (T2R1) (Q2AB83)
Organism: Gallus gallus (Chicken)
Function: Bitter taste receptor. Binds quinine, dextromethorphan, diphenhydramine, diphenidol, chlorpheniramine, diphenidol, chloramphenicol, chloroquine and coumarin, this latter being a weak agonist, as well as epiquinidine, ethylhydrocupreine and quinidine.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255|RuleBase:RU004424}.
Interaction partners:
Sequence:
MSSLFSSFCLVIAIFESVVGLLGNGTIVAVSSTSCIRSKILSSYDVIVIFLSLSRFFLQLWMILDFLLIFFCQPSYYEENLFVTFKTVFIFLNSYSFWFAAWLSVFYCVKVASFTQSFLSWLKQRIASLIPWMLITSSLFSFATSLPFFWDSYNAHSNFTTPLTMTNSSKRITTRKTNLIFLILLCNVGIALPSIMLVFSSILLIRSLWRHTRQMQNNATGFRDPSLEALIGAIKTVFSFLLLYITNFIALILILSDTFVPLSTEEAICVVVVAACPAGQSMVLIWSNPRFRELLSSILHYVNSCVRARCS
Protein: Protein mono-ADP-ribosyltransferase TIPARP (EC 2.4.2.30) (TCDD-inducible poly(ADP-ribose) polymerase) (A0A0R4IVH6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MQEAVDTAEPALALPMGTGEFTEQQMGLADKIPLVKPCFKKKHAQRKLDTKCLRALEDPILSTLLSSDALVSGDGVFVPRNPPRPQRNICTAAVEKQSRISQVCLKEEDESTDADVAASELAVEQKVTDIQRVSIDANERRFPPQERDEAAPPSDVSGSKLNDIYTAETLQGANCLAIKEGEIFQDKSEEASLDLVFELLTQLQYHTHQGDAVSICVDFLQGVCVYGSDCAQHHTVLPYHWQIRRVDTQIWQSISDDSQEQLERLYCNPDNEHVRLKFLGRVFTLDFSAMRVCDLEFDLVRRLSTPSSSTSTTTPTNTSPTPNCLTVWKYYCRDNFGWREYSEPVVRLIEEASGRGLKEVRFITLQNQYILNIREGFQQNAVFGFRRQIKKRPLFRSSIMLTPYLQTLGGLSSAFLSSLETSGNQPLSPTSSTPSKMYPETWLPMNNCQDFMRVPVSRDDRSYRTVYSLFHKTVSETKFRILKILRVQNPFLWEKYKRKKEYMSRRMTDMDRMLNERHLFHGTSQDVVEGICKHNFDPRVCGKHATMFGQGSYFARKAVYSHNFSKRSPNGVHYMFLAKVLTGKFTVGNPSMRRPPPLNPRDASSDLFDSCVDNWMDPQIFVIFNDDQSYPYFIVQYEEVGSTVAI
Protein: ORM1-like protein 1 (Q921I0)
Organism: Mus musculus (Mouse)
Function: Negative regulator of sphingolipid synthesis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9P0S3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9P0S3}.
Interaction partners:
- Serine palmitoyltransferase 1
- Serine palmitoyltransferase small subunit A
- Serine palmitoyltransferase 2
- Serine palmitoyltransferase 3
- Serine palmitoyltransferase small subunit B
- Predicted gene 6993
Sequence:
MNVGVAHSEVNPNTRVMNSRGMWLTYALGVGLLHIVLLSIPFCSVPVAWTLTNIIHNLGMYVFLHAVKGTPFETPDQGRARLLTHWEQLDYGVQFTSSRKFFTISPIILYFLASFYTKYDPTHFILNTASLLSVLIPKMPQLHGVRIFGINKY
Protein: Cullin, a subunit of E3 ubiquitin ligase (O53421)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
Sequence:
MGAQPFIGSEALAAGLISWHELGKYYTAIMPNVYLDKRLKPSLRQRVIAAWLWSGRKGVIAGASASALHGAKWVDDHALVELIWRNARAPNGVRTKDELLLDGEVQRLCGLTVTTVERTAFDLGRRPPLGQAITRLDALANATDFKINDVRELARKHPHTRGLRQLDKALDLVDPGAQSPKETWLRLLLINAGFPRPSTQIPLLGVYGHPKYFLDMGWEDIMLAVEYDGEQHRLSRDQFVKDVERLEYIRRAGWTHIRVLADHKGPDVVRRVRQAWDTLTSRR
Protein: Trypanothione reductase (EC 1.8.1.12) (N(1),N(8)-bis(glutathionyl)spermidine reductase) (Q389T8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Trypanothione synthetase, putative
- Thioredoxin
- protein disulfide-isomerase
- 2-oxoisovalerate dehydrogenase subunit alpha
- 3-methyl-2-oxobutanoate dehydrogenase
- Pyruvate dehydrogenase E1 component subunit beta
- Nucleoside diphosphate kinase-like domain-containing protein
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
Sequence:
MSKAFDLVVIGAGSGGLEAGWNAATLYGKRVAVVDVQTSHGPPFYAALGGTCVNVGCVPKKLMVTGAQYMDHLRESAGFGWEFDGSSVKANWKKLIAAKNEAVLDINKSYEGMFNDTEGLDFFLGWGSLESKNVVVVRETADPKSAVKERLQADHILLATGSWPQMPAIPGIEHCISSNEAFYLPEPPRRVLTVGGGFISVEFAGIFNAYKPPGGKVTLCYRNNLILRGFDETIREEVTKQLTANGIEIMTNENPAKVSLNTDGSKHVTFESGKTLDVDVVMMAIGRIPRTNDLQLGNVGVKLTPKGGVQVDEFSRTNVPNIYAIGDITDRLMLTPVAINEGAALVDTVFGNKPRKTDHTRVASAVFSIPPIGTCGLIEEVAAKEFEKVAVYMSSFTPLMHNISGSKYKKFVAKIVTNHSDGTVLGVHLLGDGAPEIIQAVGVCLRLNAKISDFYNTIGVHPTSAEELCSMRTPSYYYVKGEKMEKLPDSNL