wanglab/gogpt-training-data huggingface dataset:
Protein: Serine/threonine-protein phosphatase 4 catalytic subunit 1 (PP4C-1) (EC 3.1.3.16) (Q9XW79)
Organism: Caenorhabditis elegans
Function: Protein phosphatase which plays an essential role in meiosis and in early embryonic mitosis. During spermatocyte meiosis and the first embryonic mitosis, regulates centrosome maturation, and thus spindle formation, by recruiting some of the components of the pericentriolar material (PCM). During oocyte meiosis I, regulates meiotic chromosome dynamics including synapsis-independent chromosome pairing, restriction of synapsis to homologous chromosomes, programmed DNA double-strand break initiation and crossover formation resulting in chiasma formation. During oocyte meiosis II and probably together with regulatory subunit ppfr-1, may regulate microtubule severing by dephosphorylating and activating mei-1, a component of the katanin microtubule severing complex.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11896188}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:11896188}. Note=Localizes at centrosomes from prophase to telophase but not during interphase. Also localizes to the cytoplasm throughout the cell cycle. {ECO:0000269|PubMed:11896188}.
Interaction partners:
- Serine/threonine-protein phosphatase 4 regulatory subunit ppfr-4
- Protein Phosphatase Four Regulatory subunit
- Serine/threonine-protein phosphatase 4 regulatory subunit 3-like central domain-containing protein
- Serine/threonine-protein phosphatase 4 regulatory subunit 1
- Serine/threonine-protein phosphatase 2A activator
- Serine/threonine-protein phosphatase 4 regulatory subunit 4
- Probable serine/threonine-protein phosphatase PP2A regulatory subunit
- TIP41-like protein
- Serine/threonine-protein phosphatase 2A regulatory subunit sur-6
- Transcription elongation factor SPT5
Sequence:
MALACTDSANSTFSRVDSPTSGPSDQLTTHDLDRHIEKLMRCELIAEQDVKTLCAKAREILAEEGNVQVIDSPVTICGDIHGQFYDLMELFKVGGPVPNTNYLFLGDFVDRGFYSVETFLLLLALKARYPDRMMLIRGNHESRQITQVYGFYDECLRKYGNASVWKHCTEVFDYLSLAAVIDGKVFCVHGGLSPSISTMDQIRVIDRKQEVPHDGPMCDLLWSDPEEGNVGWGLSPRGAGYLFGADASKTFCETNGVDLICRAHQLVMEGYKWHFNEKVLTVWSAPNYCYRCGNVAAILELDENLNKEFTIFEAAPQENRGAPAKKPHADYFL
Protein: Forkhead box protein H1 (Forkhead activin signal transducer 1) (Fast-1) (xFAST-1) (XFoxH1a) (P70056)
Organism: Xenopus laevis (African clawed frog)
Function: Transcriptional activator. Recognizes and binds to the DNA sequence 5'-TGT[GT][GT]ATT-3'. Upon TGF-beta induction, forms a transcriptionally active complex with smad2 and smad4 called activin-responsive factor 1 (ARF1), which binds a site on the mix-B/mix.2 promoter called the activin response element (ARE). Binds to activated smads and the ARE with much lower affinity than fast3. Necessary for the first steps in mesoderm specification, directly inducing mesodermal genes. Acts with fast3 to control the convergent extension movements of gastrulation. Binds to the proximal element (PE) of the gsc gene and cooperates with gtf2ird1/wbscr11 and SMAD proteins to regulate gsc transcription.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089, ECO:0000269|PubMed:8878477}.
Interaction partners:
Sequence:
MRDPSSLYSGFPAGSQYESVEPPSLALLSSIDQEQLPVATGQSYNHSVQHWPQPWPPLSLYREGGTWSPDRGSMYGLSPGTHEGSCTHTHEGPKDSMAGDQTRSRKSKKKNYHRYNKPPYSYLAMIALVIQNSPEKRLKLSQILKEVSTLFPFFNGDYMGWKDSIRHNLSSSDCFKKILKDPGKPQAKGNFWTVDVSRIPLDAMKLQNTALTRGGSDYFVQDLAPYILHNYKYEHNAGAYGHQMPPSHARSLSLAEDSQQTNTGGKLNTSFMIDSLLHDLQEVDLPDASRNLENQRISPAVAMNNMWSSAPLLYTHSKPTRNARSPGLSTIHSTYSSSSSSISTISPVGFQKEQEKSGRQTQRVGHPIKRSREDDDCSTTSSDPDTGNYSPIEPPKKMPLLSLDLPTSYTKSVAPNVVAPPSVLPFFHFPRFTYYNYGPSPYMTPPYWGFPHPTNSGGDSPRGPQSPLDLDNMLRAMPPNKSVFDVLTSHPGDLVHPSFLSQCLGSSGSPYPSRQGLM
Protein: ELM2 domain-containing protein (Q9NF71)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MSQLMNAHDRRNEPAPNAPPEFQLQNRTRPAPTPIEYITLSSDDEIEVIPPPPKRAKMMEEQKPKDLLENPQLPEVPSSSASFVIPQIVVDNEEVPEDPRMKTPSPIQGASVAMPVRARIQESPKVSRDPTPLSRASSVVIPEVPAVSEPEPLPVEVLAISIPTTSPDTAPSTSSSVETVESVTEVVAISSAEASSDAPARSPLKKKVANSVKPVVLPSRKSTRNKKDMNQIKEDEELVSNFNNGIGVISRGTIVPRGLSRTPFHFKKEATDDKAGKVKDMLKIDMQPVFTPAGHSSKDLIKRKARNSLEPSTSDADISFMKNERGKIRTGEKFQATIPDIEPSSTLTEYMDQEDKEEIFWETLDMDKDNLEESKKFHETLRNVYWRAIWRQFQGHIPFETALQHLMKNNLDFAQSLETIDENLKSLPQSFKEPCVAQVKIFDKLLQDKKTTRRQLQEKAMRNYHIAEVQQYHYRFRKFFKYQEKYGVVCNCAEKLCNNLKFEPRYGCTNCKKNVKSSSDHGATEKLCLICQTYQKLTGNVRPARNVEFCDDELEKIYHWSQKEEDLNRTLSREEFEELVREEKNKKWKNNDLSAEETAMLNQKELRIPNRRHRTHLSDQEKQARGEKICAQLQPYVLPHFSKCNCKRMGRSSWRCETEGKSSFSIQERKDYFREVRDCKGDLQQVARNLKVAPEVVRAFINIYGIEYDLEIYFPNKKLPNLIPIVYDIPPSNLPPIIPDGSSNSSSRDGSPYIPPEERSPKKRRSN
Protein: Crp/Fnr family transcription regulator protein (D8IWL7)
Organism: Herbaspirillum seropedicae (strain SmR1)
Interaction partners:
- Coproporphyrinogen-III oxidase
- Adenylate cyclase protein
Sequence:
MSSLPASTHKHSPPPVNLHALRASCSACSMHQLCLPMGLDQGDMQRLEQVINRRRKVKRDETLYRLNDKFDMLYAIRLGHFKTFQHNPNGGQQITGFQMAGELLGMDAIGAGHHLCEAVALEDSEVCEIPFASLEDLFRDMPTLLRQFHRMMSLEISREQRVMLTLGSMTAQQKMAAFLLNLSSRYMSRGYSSTRFQLRMTREEIGNYLGLAVESVSRLLTNFKKSGVIEVNHRDVELCDLPTLRAVALGNDPCA
Protein: Glycine cleavage system H protein 3, mitochondrial (Q9LQL0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The glycine decarboxylase (GDC) or glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein (By similarity).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14671022, ECO:0000305|PubMed:25862457}.
Interaction partners:
- Aminomethyltransferase, mitochondrial
- Glycine dehydrogenase
- Glycine dehydrogenase
- Dihydrolipoyl dehydrogenase 2, chloroplastic
- Dihydrolipoyl dehydrogenase 1, chloroplastic
- Glycine cleavage system H protein 1
- Dihydrolipoyl dehydrogenase 1, mitochondrial
- Dihydrolipoyl dehydrogenase 2, mitochondrial
- Serine--glyoxylate aminotransferase
- Serine hydroxymethyltransferase 1, mitochondrial
Sequence:
MALRMWASSTANALKLSSSASKSHLLPAFSISRCFSSVLEGLKYANSHEWVKHEGSVATIGITDHAQDHLGEVVFVELPEANSSVSKEKSFGAVESVKATSEILSPISGEVIEVNTKLTESPGLINSSPYEDGWMIKVKPSSPAELEALMGPKEYTKFCEEEDAAH
Protein: Serine rich endogenous peptide 14 (AtSCOOP14) (Phytocytokine SCOOP14) (Precursor of serine rich endogenous peptide phytocytokine 14) (Secreted transmembrane peptide 2) (A0JQ18)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Brassicaceae-specific phytocytokine (plant endogenous peptide released into the apoplast) perceived by MIK2 in a BAK1/SERK3 and SERK4 coreceptors-dependent manner, that modulates various physiological and antimicrobial processes including growth prevention and reactive oxygen species (ROS) response regulation. Inhibits root growth and regulates root meristems. Prevents general growth and development. Exhibits antibacterial effects against Pseudomonas syringae pv. tomato DC3000, Ralstonia solanacearum, Bacillus subtilis and Agrobacterium tumefaciens, thus being an antimicrobial peptide (AMP).
Subcellular location: Cell membrane {ECO:0000269|PubMed:31001913}. Secreted, extracellular space, apoplast {ECO:0000269|PubMed:31001913}. Note=The precursor of SCOOP14, PROSCOOP14, accumulates at the plasma membrane and is proteolytically cleaved to release the SCOOP14 in the apoplasm. {ECO:0000269|PubMed:31001913}.
Interaction partners:
Sequence:
MAAKTSNLVALLLSLFLLLLSISSQVGLGEAKRNLRNNLRLDCVSHPSPPPPHRSMAPPIFVPPSTSHKGQGP
Protein: Prolyl 4-hydroxylase subunit alpha-1 (4-PH alpha-1) (EC 1.14.11.2) (Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-1) (Q60715)
Organism: Mus musculus (Mouse)
Function: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
Subcellular location: Endoplasmic reticulum lumen.
Interaction partners:
- Protein disulfide-isomerase
- Prolyl 4-hydroxylase subunit alpha-2
- Proline dehydrogenase 1, mitochondrial
- Prolyl 4-hydroxylase subunit alpha-3
- Hydroxyproline dehydrogenase
- Pyrroline-5-carboxylate reductase 3
- Pyrroline-5-carboxylate reductase 2
- Cytosol aminopeptidase
- Pyrroline-5-carboxylate reductase 1, mitochondrial
- Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2
Sequence:
MIWVVLMMAILLPQSLAHPGFFTSIGQMTDLIHNEKDLVTSLKDYIKAEEDKLEQIKKWAEKLDRLTSTATKDPEGFVGHPVNAFKLMKRLNTEWSELENLILKDMSDGFISNLTIQRQYFPNDEDQVGAAKALFRLQDTYNLDTNTISKGNLPGVQHKSFLTAEDCFELGKVAYTEADYYHTELWMEQALTQLEEGELSTVDKVSVLDYLSYAVYQQGDLDKALLLTKKLLELDPEHQRANGNLVYFEYIMSKEKDANKSASGDQSDQKTAPKKKGIAVDYLPERQKYEMLCRGEGIKMTPRRQKRLFCRYHDGNRNPKFILAPAKQEDEWDKPRIIRFHDIISDAEIEIVKDLAKPRLRRATISNPVTGALETVHYRISKSAWLSGYEDPVVSRINMRIQDLTGLDVSTAEELQVANYGVGGQYEPHFDFARKDEPDAFRELGTGNRIATWLFYMSDVSAGGATVFPEVGASVWPKKGTAVFWYNLFASGEGDYSTRHAACPVLVGNKWVSNKWLHERGQEFRRPCTLSELE
Protein: Pyridoxamine 5'-phosphate oxidase N-terminal domain-containing protein (A0A0H3LAC5)
Organism: Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman)
Interaction partners:
Sequence:
MAMVNTTTRLSDDALAFLSERHLAMLTTLRADNSPHVVAVGFTFDPKTHIARVITTGGSQKAVNADRSGLAVLSQVDGARWLSLEGRAAVNSDIDAVRDAELRYAQRYRTPRPNPRRVVIEVQIERVLGSADLLDRA
Protein: Transaminase BacF (EC 2.6.1.-) (Transaminase A) (P39643)
Organism: Bacillus subtilis (strain 168)
Function: Part of the bacABCDEF operon responsible for the biosynthesis of the nonribosomally synthesized dipeptide antibiotic bacilysin, composed of L-alanine and L-anticapsin. Bacilysin is an irreversible inactivator of the glutaminase domain of glucosamine synthetase. Catalyzes the reductive amination of the C2 ketone of tetrahydro-hydroxyphenylpyruvate (H4HPP), with L-Phe as an amino donor, to yield tetrahydrotyrosine (H4Tyr) diastereomer. D-Phe is not an effective amino donor. BacF associated to BacG converts 3E,7R- and 3Z,7R-ex-H2HPP to 2S,4R,7R- and 2S,4S,7R-H4Tyr, respectively. Given that bacilysin has the 2S,4S stereochemistry in its anticapsin moiety, it is likely that the 2S,4S-H4Tyr is the diastereomer used for the biosynthesis.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Dihydroanticapsin 7-dehydrogenase
- Putative bacilysin exporter BacE
- H2HPP isomerase
- L-lactate dehydrogenase
- Alanine--anticapsin ligase
- NADPH-dependent reductase BacG
- Prephenate decarboxylase
- Glutathione peroxidase homolog BsaA
- HTH-type transcriptional regulatory protein GabR
- 2-oxoglutaramate amidase
Sequence:
MEITPSDVIKTLPRQEFSLVFQKVKEMEKTGAHIINLGQGNPDLPTPPHIVEALREASLNPSFHGYGPFRGYPFLKEAIAAFYKREYGVTINPETEVALFGGGKAGLYVLTQCLLNPGDIALVPNPGYPEYLSGITMARAELYEMPLYEENGYLPDFEKIDPAVLEKAKLMFLNYPNNPTGAVADAAFYAKAAAFAKEHNIHLIHDFAYGAFEFDQKPASFLEAEDAKTVGAELYSFSKTFNMAGWRMAFAVGNEKIIQAVNEFQDHVFVGMFGGLQQAASAALSGDPEHTESLKRIYKERIDFFTALCEKELGWKMEKPKGTFYVWAEIPNTFETSHQFSDYLLEHAHVVVTPGEIFGSNGKRHVRISMVSKQEDLREFVTRIQKLNLPFGSLQETSR
Protein: Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (SMAD family member 3) (SMAD 3) (Smad3) (P84023)
Organism: Gallus gallus (Chicken)
Function: Transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinase. SMAD3 is a receptor-regulated SMAD (R-SMAD) (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P84022}. Nucleus {ECO:0000250|UniProtKB:P84022}. Note=In the cytoplasm in the absence of ligand. Migration to the nucleus when complexed with SMAD4. {ECO:0000250|UniProtKB:P84022}.
Interaction partners:
- Mothers against decapentaplegic homolog
- TGF-beta receptor type-1
- Transforming growth factor beta-1 proprotein
- Activin receptor type-1
- Fork-head domain-containing protein.
- E2F transcription factor 4
- Interleukin-1
- Zinc finger FYVE domain-containing protein
- Receptor protein serine/threonine kinase
- Mothers against decapentaplegic homolog
Sequence:
MSSILPFTPPIVKRLLGWKKGEQNGQEEKWCEKAVKSLVKKLKKTGQLDELEKAITTQNINTKCITIPRSLDGRLQVSHRKGLPHVIYCRLWRWPDLHSHHELRAMEMCEYAFNMKKDEVCVNPYHYQRVETPVLPPVLVPRHTEIPAEFPPLDDYSHSIPENTNFPAGIEPQSNYIPETPPPGYLSEDGETSDHQMNPSMDAGSPNLSPNPMSPAHNNLDLQPVTYCEPAFWCSISYYELNQRVGETFHASQPSMTVDGFTDPSNSERFCLGLLSNVNRNAAVELTRRHIGRGVRLYYIGGEVFAECLSDSAIFVQSPNCNQRYGWHPATVCKIPPGCNLKIFNNQEFAALLAQSVNQGFEAVYQLTRMCTIRMSFVKGWGAEYRRQTVTSTPCWIELHLNGPLQWLDKVLTQMGSPSIRCSSVS
Protein: Cytochrome P450 703A2 (EC 1.14.14.130) (Protein DEFECTIVE IN EXINE FORMATION 2) (Q9LNJ4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in pollen wall development. Catalyzes the conversion of medium-chain saturated fatty acids to the corresponding monohydroxylated fatty acids, with a preferential hydroxylation of lauric acid at the C-7 position. In-chain hydroxylated fatty acids, together with omega-hydroxylated fatty acids, are key monomeric aliphatic building blocks for sporopollenin synthesis during exine formation.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- 4-coumarate--CoA ligase-like 1
- Type III polyketide synthase B
- ABC transporter G family member 26
- Type III polyketide synthase A
- Tetraketide alpha-pyrone reductase 2
- Tetraketide alpha-pyrone reductase 1
- Transcription factor MYB35
- Transcription factor MYB80
- Short-chain dehydrogenase reductase ATA1
- Protein DEFECTIVE IN EXINE FORMATION 1
Sequence:
MILVLASLFAVLILNVLLWRWLKASACKAQRLPPGPPRLPILGNLLQLGPLPHRDLASLCDKYGPLVYLRLGNVDAITTNDPDTIREILLRQDDVFSSRPKTLAAVHLAYGCGDVALAPMGPHWKRMRRICMEHLLTTKRLESFTTQRAEEARYLIRDVFKRSETGKPINLKEVLGAFSMNNVTRMLLGKQFFGPGSLVSPKEAQEFLHITHKLFWLLGVIYLGDYLPFWRWVDPSGCEKEMRDVEKRVDEFHTKIIDEHRRAKLEDEDKNGDMDFVDVLLSLPGENGKAHMEDVEIKALIQDMIAAATDTSAVTNEWAMAEAIKQPRVMRKIQEELDNVVGSNRMVDESDLVHLNYLRCVVRETFRMHPAGPFLIPHESVRATTINGYYIPAKTRVFINTHGLGRNTKIWDDVEDFRPERHWPVEGSGRVEISHGPDFKILPFSAGKRKCPGAPLGVTMVLMALARLFHCFEWSSPGNIDTVEVYGMTMPKAKPLRAIAKPRLAAHLYT
Protein: MARVEL domain-containing protein (Q18089)
Organism: Caenorhabditis elegans
Interaction partners:
- Serpentine Receptor, class H
- Receptor L-domain domain-containing protein
- FAM192A_Fyv6_N domain-containing protein
- Uncharacterized protein
- Copine family protein 2
Sequence:
MAYKDMMEMPGVLKPALLLLTLLQIIFMASPGVRGWFWFICLTSILEFLAAIAVVAVVFLDLTFTRSGQFVIIELAYSGAFCVCSALNTIYYFCNIFYHFNFWFLLATIVSVLLVLAYGLQALMAWTSMSASRTSSSHTSNQATAGPPPTVYPAGANPA
Protein: Os05g0594700 protein (cDNA clone:J033048M19, full insert sequence) (Q5TKG1)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MATVSDIGLSAAINVSMAVAFLLVFAFLRLQPINDRVYFPKWYLRGMRDSPVSSGAAVQKVVNLNMRSYLKFLSWMPAALKMPEDELINHAGLDSAVYLRIYLTGIKIFVPISILASLVLFPVNWTNDTLDSMKVVHSKIDKLSISNIPYGSNRFVTHLVMAYAVTFWTCYVLFREYEIITTMRLRFLASEKRRPDQFTVLVRNIPPDPDESISELVEHFFLVNHPDHYLRHQVVYNANKLADLVEKKKKLQNWLDYYQLKYERNPSKRPTTKTGFLGCFGSEVDAIEYYKAEIEKIGKEEADERQKIMKDPQSAVPAAFVSFRSRWGAAVCAQTQQTSNPTVWITEWAPEPRDVYWNNLSIPFVSLTVRRLIVAVAFFFLNFFYVIPIAFVQSLASLEGIEKALPFLKPLIKIDVIKSFIQGFLPGIALKVFLILLPTILMFMSKFEGLISQSSLERRSASKYYIFLFFNVFLGSIVTGSALDQLKAYIHQSANEIPRTIGVAIPMRATFFITYVMVDGWTGVAGEILRLRALIIFHLKNFFLVKTEKDREEAMDPGSICFDWCEPRIQLYFLLGLVYAVVTPLLLPFILVFFGLAYVVYRHQIINVYNQQYESGAQFWPSVHGRIIIALIVSQLLLIGLLSTKGFEETTPVLVVLPVLTFWFYKYCKNRFEPAFVRNPLQEAMRKDTLERAREPTFDLKAYLANAYLHPVFKGREEEDNMSISEDVGMEEVIVPTKRQSRRNTPAQSKYEGSDTLSLPETVHER
Protein: Elongation factor 2 (Q582T0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Diphthine--ammonia ligase
- Eukaryotic translation initiation factor 5A
- Large ribosomal subunit protein uL5
- 40S ribosomal protein S15a, putative
- 60S ribosomal protein L5, putative
- 40S ribosomal protein S18, putative
- Small ribosomal subunit protein uS5
- 40S ribosomal protein S5, putative
- 60S ribosomal protein L17, putative
Sequence:
MNLETTEHLQRLGQEPERIRNFCVVAHVDHGKTTLSDYLVASNGILSPQLAGEVRLLDSRPDEQERRITMKASSVVLRHLHEGVEHLLNLVDSPGHIDFSCEVSTAMRLCDGAVVIVDVVDGVTQQSNGILRHAYREGLSMCLVLNKVDLLITVQQLSPEEAYYRMRSIVETCNAALAGFANQLKIQEEDCVAGKERDDPSDDVWFCPTKGNVLFASCHDGWAFSAEFFSRLYEGKLGVPDLQKHLWGEYYLKPQMKGVDTTPRRAGQQTLAVQLMLEPIWKLYSVFLDEKDDGPEKQLSMAAKLGIPEKLWNNPRRGQRGKLKALLSSWMPLAKCVLSTVCSKLDSPVSAQRRRLRFLIPRFDEAPTAVREALMNCSPAPDVPCVVYVCKLVDTQFLVGTTLGREGNDDDAFIGFARVYSGRLRPGMKMYVHSDDKVVEATVGKVFLFRGAGLDEADEVCSGTLCGVGGLTPYIAKYATLSSLEGVPPLNPLVLPSTSIVRASVFPRDPKDLFLLQQGLRLLYKVDPQVEVSILPTGEHVIGTAGEVHMERCLRDLIDTFARVEVMVSESIVSFRETIVATGPSAKPKLHTATTPDGAFAVTLYARCMPQEVLDIIKDDNKNRGTAGHVIQRIGGALNANKRWSKEIEHGVVACGPQKLKFVGVTLLLNFSEHTDSLGVLQRFNHWKDSIVAGFQAAAESGPMAQEPMFNIAFVITDINVEASTSLTGGMVLPCVRDACRAAMELHSRRLVEPVYECTVYSSGATQGKIYGSLSRRRSDIIEEVPNEGSDLFYIRCLLPAVEAFGLQDELRVVTQGASTAQLQMSHWNVLDADPYFTPTTREEIEEHGAEVATKNIAEQLLERVRRRKGLHRERVVENAEKQKFSLKGA
Protein: Large ribosomal subunit protein bL17m (39S ribosomal protein L17, mitochondrial) (L17mt) (MRP-L17) (Q3T0L3)
Organism: Bos taurus (Bovine)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:10593885, ECO:0000269|PubMed:16510155}.
Interaction partners:
- Large ribosomal subunit protein bL32m
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein uL22m
- Ribosomal protein
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein bL20m
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein uL5
- Small ribosomal subunit protein uS4
Sequence:
MRLSFAAAISHGRVYRRLGLGPESRIHLLQNLLTGLVRHERIEASWARVDELRGYAEKLIDYGKLGDTNERAMRMADFWLTEKDLIPKLFQVLAPRYQGQNGGYTRMLQIPNRNQQDRAKMAVIEYKGNCLPPLPLPRRDSNLTLLNQLLRGLRQDQEASTRSSHPAQTPEV
Protein: cGMP-dependent 3',5'-cyclic phosphodiesterase (EC 3.1.4.17) (Cyclic GMP-stimulated phosphodiesterase) (CGS-PDE) (cGSPDE) (Q922S4)
Organism: Mus musculus (Mouse)
Function: cGMP-activated cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. Has a higher efficiency with cGMP compared to cAMP (By similarity). Plays a role in cell growth and migration (By similarity).
Subcellular location: [Isoform PDE2A1]: Cytoplasm {ECO:0000250|UniProtKB:O00408}.; SUBCELLULAR LOCATION: [Isoform PDE2A2]: Mitochondrion matrix {ECO:0000269|PubMed:21724846}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:O00408}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:O00408}.; SUBCELLULAR LOCATION: [Isoform PDE2A3]: Cell membrane {ECO:0000250|UniProtKB:O00408}; Lipid-anchor {ECO:0000250|UniProtKB:O00408}.
Interaction partners:
- Adenosine kinase
- Inosine triphosphate pyrophosphatase
- Adenine phosphoribosyltransferase
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Guanylate kinase
- GTP:AMP phosphotransferase AK3, mitochondrial
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Deoxycytidine kinase
- Hypoxanthine-guanine phosphoribosyltransferase
- Adenylosuccinate lyase
Sequence:
MGQACGHSILCRSQQYPAARPAEPRGQQVFLKPDEPPPQPCADSLQDALLSLGAVIDIAGLRQAARDALSAVLPKVETVYTYLLDGESRLVCEDPPHELPQEGKIREAVISQKRLSCNGLGPSDLLGKPLARLVAPLAPDMQVLVIPLLDKETGSVAAVILVHCGQLSDSEEQSLQVVEKHALVALRRVQALQQRRPEAVQNTSVDASEDQKDEKGYTDHDRKILQLCGELFDLDATSLQLKVLQYLQQETQATHCCLLLVSEDNLQLSCKVIGDKVLGEEVSFPLTMGRLGQVVEDKQCIQLKDLTSDDVQQLQNMLGCELQAMLCVPVISRATDQVVALACAFNKLGGDFPTSSFTDEDEHVIQHCFHYTGTVLTSTLAFQKEQKLKCECQALLQVAKNLFTHLDDVSVLLQEIITEARNLSNAEICSVFLLDQNELVAKVFDGGVVDDESYEIRIPADQGIAGHVATTGQILNIPDAYAHPLFYRGVDDSTGFRTRNILCFPIKNENQEVIGVAELVNKINGPWFSKFDEDLATAFSIYCGISIAHSLLYKKVNEAQYRSHLANEMMMYHMKVSDDEYTKLLHDGIQPVAAIDSNFANFTYTPRSLPEDDTSMAILSMLQDMNFINNYKIDCPTLARFCLMVKKGYRDPPYHNWMHAFSVSHFCYLLYKNLELSNYLEDIEIFALFISCMCHDLDHRGTNNSFQVASKSVLAALYSSEGSVMERHHFAQAIAILNTHGCNIFDHFSRKDYQRMLDLMRDIILATDLAHHLRIFKDLQKMAEVGYDRNNRQHHRLLLCLLMTSCDLSDQTKGWKTTRKIAELIYKEFFSQGDLEKAMGNRPMEMMDREKAYIPELQISFMEHIAMPIYKLLQDLFPKAAELYERVASNREHWTKVSHKFTIRGLPSNNSLDFLDEEYEVPDLDGTRAPVNGCCSLEG
Protein: Protein naked cuticle homolog 1 (Naked-1) (Q2TJA6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Cell autonomous antagonist of the canonical Wnt signaling pathway. May activate a second Wnt signaling pathway that controls planar cell polarity (By similarity).
Subcellular location: Cell membrane {ECO:0000250}. Cytoplasm {ECO:0000250}.
Interaction partners:
- Dishevelled segment polarity protein 2.
- Dishevelled segment polarity protein 3b
- Dishevelled segment polarity protein 3a
- Dishevelled segment polarity protein 1b
- Dishevelled segment polarity protein 1a.
- Protein naked cuticle homolog 2-like
- Axin-2
- Dapper homolog 1
Sequence:
MGKLHSKHAAICKARESPEGDSFVVNACLARKGLDDWMVKQKYYCSSSRVDQRDCQQKNNCELSPRDPLDEGYAEGISDEHYRLEVALPPEKTDSCSVEERMQGTEGSATVGPHKQLQFEELECAVSVEEDNRQEWTFTLYDFDNNGKVTREDITSLLHTIYEVVDASVNHSPSSSKTLRVKLSVAPDSSQRWKNCTQTNTDTPNPKHKGEKCIEDSKTSEKKSRAFLRRYHAEHHSQQGCQRHCVDENLERRNHYLDLAGIENYTSRFGTAAPATEPAKPTHATRSSNQSRSRSQEPENGQVHPAHHRRSQTMSTDPPAILTRHTHALRSPKTHRTPPTQASAGRVMRRGAPPPPSVPNQTPPHQSSGPYRRHKQRPKEALHYRALGPSVTSGPVLEKEHVRDLPSLVLYEGGLAQVVQRHEHHHHHEHHHHYHHFYQS
Protein: Kin of rumpel, isoform D (LP24461p) (Q9VBK1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- FI19011p1
- Small ribosomal subunit protein uS10m
Sequence:
MSTTADPVALGVNSPVEDVVAKTTTTVANAIAKTVAVISSTVSTSSTTGATSTISTSSSTPTTSTTFAYTPTPTPTQSASPSLEDGEEKLSVKDLSQALQHFGIVDYLVFIAMLAVCAVIGFYFGFIEKKQKKQKLAGKDGGGAAGVEERRGSEALDYLVGGRQMKVFPVALSLVASFVSGISLLGTSTEIYVYGTQYAFILVTLAISGAISWYIFLPVFCNLQLTSTYEYFERRFDRRVRIFGSCLFVVMNILWQPICIYVPALTLNQVSGISVSKIVPVTSFICILYTSVGGIKGVVWTDVIQGTVMIGSMLIVIIKGTLDLGGLSVVLDHNRQYDRLVGPDMTFDPTARMGVFALFVGGALFKLQANGINQAIVQRYLTLPNNKDVKKALVLSLIGFMFVMLMCVYIGLLAFAEFYHCDPITTGLARAKDQVIPLYVVKNVGHIPGLVGLFVAGVFSAALSSLSTALNSLSGVILTDFVEPFRKKPLTERQTAYLLRGVVISFGLISMASVPIVQRLGLVMQLSSTVAAITCGPLLGAFSVGMLLPFVKTESLLTGISCASSFTAYIVVRAQIAIFTGSLTFPAKPVSIQDCDYTFDLPANWNATTTATPTESTSHGIHEISFLWYTAVGSVGTVLGSLLATLYFGRQDPRVVDKELISPVLRKFWYGKYESVASEEKNNFNLHESETQLKLEQP
Protein: cDNA FLJ13016 fis, clone NT2RP3000624, moderately similar to Rattus norvegicus SECIS binding protein 2 (sbp2 gene) (Q9H948)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLTALEKKQHSQHAKQSSKPVVVSVGAVPVLSKECASGERGRRMSQMKTPHNPLDSSAPLMKKGKQREIPKAKKPTSLKKIILKERQERKQRLQENAVSPAFTSDDTQDGESGGDDQFPEQAELSGPEGMDELISTPSVEDKSEEPPGTELQRDTEASHLAPNHTTFPKIHSRRFRDYCSQMLSKEVDACVTDLLKELVRFQDRMYQKDPVKAKTKRRLVLGLREVLKHLKLKKLKCVIISPNCEKIQSKGGLDDTLHTIIDYACEQNIPFVFALNRKALGRSLNKAVPVSVVGIFSYDGAQDQFHKMVELTVAARQAYKTMLENVQQELVGEPRPQAPPSLPTQGPSCPAEDGPPALKEKEEPHYIEIWKKHLEAYSGCTLELEESLEASTSQMMNLNL
Protein: cDNA FLJ56483, highly similar to Eukaryotic translation initiation factor 4 gamma 1 (B4DSI9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MMIPSQISYPASQGAYYIPGQGRSTYVVPTQQYPVQPGAPGFYPGASPTEFGTYAGAYYPAQGVQQFPTGVAPAPVLMNQPPQIAPKRERKTIRIRDPNQGGKDITEEIMSGARTASTPTPPQTGGGLEPQANGETPQVAVIVRPDDRSQGAIIADRPGLPGPEHSPSESQPSSPSPTPSPSPVLEPGSEPNLAVLSIPGDTMTTIQMSVEESTPISRETGEPYRLSPEPTPLAEPILEVEVTLSKPVPESEFSSSPLQAPTPLASHTVEIHEPNGMVPSEDLEPEVESSPELAPPPACPSESPVPIAPTAQPEELLNGAPSPPAVDLSPVSEPEEQAKEVTASMAPPTIPSATPATAPSATSPAQEEEMEEEEEEEEGEAGEAGEAESEKGGEELLPPESTPIPANLSQNLEAAAATQVAVSVPKRRRKIKELNKKEAVGDLLDAFKEANPAVPEVENQPPAGSNPGPESEGSGVPPRPEEADETWDSKEDKIHNAENIQPGEQKYEYKSDQWKPLNLEEKKRYDREFLLGFQFIFASMQKPEGLPHISDVVLDKANKTPLRPLDPTRLQGINCGPDFTPSFANLGRTTLSTRGPPRGGPGGELPRGPAGLGPRRSQQGPRKEPRKIIATVLMTEDIKLNKAEKAWKPSSKRTPADKDRGEEDADGSKTQDLFRRVRSILNKLTPQMFQQLMKQVTQLAIDTEERLKGVIDLIFEKAISEPNFSVAYANMCRCLMALKVPTTEKPTVTVNFRKLLLNRCQKEFEKDKDDDEVFEKKQKEMDEAATAEERGRLKEELEEARDIARRRSLGNIKFIGELFKLKMLTEAIMHDCVVKLLKNHDEESLECLCRLLTTIGKDLDFEKAKPRMDQYFNQMEKIIKEKKTSSRIRFMLQDVLNLRGSNWVPRRGDQGPKTIDQIHKEAEMEEHREHIKVQQLMAKGSDKRRGGPPGPPISRGLPLVDDGGWNTVPISKGSRPIDTSRLTKITKPGSIDSNNQLFAPGGRLSWGKGSSGGSGAKPSDAASEAARPATSTLNRFSALQQAVPTESTDNRRVVQRSSLSRERGEKAGDRGDRLERSERGGDRGDRLDRARTPATKRSFSKEVEERSRERPSQPEGLRKAASLTEDRDRGRDAVKREAALPPVSPLKAALSEEELEKKSKAIIEEYLHLNDMKEAVQCVQELASPSLLFIFVRHGVESTLERSAIAREHMGQLLHQLLCAGHLSTAQYYQGLYEILELAEDVEIDIPHVWLYLAELVTPILQEGGVPMGELFREITKPLRPLGKAASLLLEILGLLCKSMGPKKVGTLWREAGLSWKEFLPEGQDIGAFVAEQKVEYTLGEESEAPGQRALPSEELNRQLEKLLKEGSSNQRVFDWIEANLSEQQIVSNTLVRALMTAVCYSAIIFETPLRVDVAVLKARAKLLQKYLCDEQKELQALYALQALVVTLEQPPNLLRMFFDALYDEDVVKEDAFYSWESSKDPAEQQGKGVALKSVTAFFKWLREAEEESDHN