wanglab/gogpt-training-data huggingface dataset:
Protein: Protein Tob1a (Transducer of ERBB2, 1a) (Q7SZR1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- CCR4-NOT transcription complex subunit 7
- Receptor protein-tyrosine kinase.
Sequence:
MQLEIQVALNFIISYLYNKLPRRRVNIFGEELERQLKQKYEGHWYPDKPYKGSGFRCIHVGEKVDPVVEQAAKESGLDIEDVRNNLPQDLSVWIDPFEVSYQIGEKGPVKVLYVDDSNDNGLELDKEIKNSFNPEAQVFMPISEPVGMSPTSSSPSPPFGQSAAVSPTFMRRSTQPLTFTTATFAATKFGSTKMKSNGRNANKVTRNSPTNLGLNVNNLLKQKAMSTSMHSLYGVGAQPQKPSALSPNAKEFVFPNLQGQGSPSAMFPGETSLNLSPLPYNNAFDVFAAYGGLNEKSLMDSLNFSLSNMQYSNQQFQPVMAN
Protein: Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q (MGpi1p) (N-acetylglucosamyl transferase component GPI1) (Phosphatidylinositol-glycan biosynthesis class Q protein) (PIG-Q) (Q9QYT7)
Organism: Mus musculus (Mouse)
Function: Part of the glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex that catalyzes the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol and participates in the first step of GPI biosynthesis.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit H
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit P
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit Y
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit C
- Protein preY
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
- N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
- Glucosaminyl-phosphatidylinositol-acyltransferase PIGW
- GPI alpha-1,6-mannosyltransferase 2
Sequence:
MVLKVFFPTCCASADSGLLVGRWVPGQSSAVILAVVHFPFIPIQVKELLAQVQKASQVPVAVLGTWCHRQQEPQESLGNFLEGLGTIFSHDPWLQLCRERGTRLWSCKATYPQMSNPLDMHPEEQVMLIFYDQRKLLLSWLHPPPVLPACQMGDTTASTGGLADIFDTVARSEVLFRNDQFDERPVRLSHWQSEGVEASILVELAKRASGPVCLLLASLLSLISAASACRLWKLWPLSFIRSKLSTCEQLHHRLKHLSFIFSTEKAQNPMQLMRKANMLVSVLLDVALGLLLLSWLHSNNRIGQLANALVPVADRVAEELQHLLQWLMGAPAGLKMNRALDQVLGRFFLYHIHLWISYIHLMSPFIEHILWHVGLSACLGLTVALSIFSDIIALLTFHIYCFYVYGARLYCLKIYGLSSLWRLFRGKKWNVLRQRVDSCSYDLDQLFIGTLLFTILVFLLPTTALYYLVFTLLRLLVITVQGLIHLLVDLINSLPLYSLGLRLCRPYRLAAGVKFRVLEKEAGRPLRLLMQINPLSYNHVMHIYRLPRCGCHPKHSWGTLCRKLVFGELIYPWRQREDKQD
Protein: Bifunctional cystathionine gamma-lyase/cysteine synthase (EC 2.5.1.47) (EC 4.4.1.1) (Beta-substituted Ala synthase 4;3) (ARAth-Bsas4;3) (L-cysteine desulfhydrase 1) (DES1) (O-acetylserine (thiol)-lyase) (OASTL) (Protein CS-LIKE) (F4K5T2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in maintaining Cys homeostasis through the desulfuration of L-cysteine. Modulates the generation of the signaling molecule sulfide in plant cytosol. Probably unable to interact with SAT and to form the decameric Cys synthase complex (CSC) and is therefore not an enzymatically true OASTL protein.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Assimilatory sulfite reductase
- Cystathionine beta-lyase, chloroplastic
- Probable cystathionine gamma-synthase 2
- L-cysteine desulfhydrase
- Probable L-cysteine desulfhydrase, chloroplastic
- Cystathionine gamma-synthase 1, chloroplastic
- Methionine gamma-lyase
- Glutamate--cysteine ligase, chloroplastic
- Serine acetyltransferase 1, chloroplastic
- Serine acetyltransferase 3, mitochondrial
Sequence:
MEDRVLIKNDVTELIGNTPMVYLNKIVDGCVARIAAKLEMMEPCSSIKDRIAYSMIKDAEDKGLITPGKSTLIEATGGNTGIGLASIGASRGYKVILLMPSTMSLERRIILRALGAEVHLTDISIGIKGQLEKAKEILSKTPGGYIPHQFINPENPEIHYRTTGPEIWRDSAGKVDILVAGVGTGGTVTGTGKFLKEKNKDIKVCVVEPSESAVLSGGKPGPHLIQGIGSGEIPANLDLSIVDEIIQVTGEEAIETTKLLAIKEGLLVGISSGASAAAALKVAKRPENVGKLIVVIFPSGGERYLSTELFESVRYEAENLPVE
Protein: Sulfofructosephosphate aldolase (SFP aldolase) (EC 4.1.2.57) (P32141)
Organism: Escherichia coli (strain K12)
Function: Cleaves 6-deoxy-6-sulfo-D-fructose 1-phosphate (SFP) to form dihydroxyacetone phosphate (DHAP) and 3-sulfolactaldehyde (SLA).
Interaction partners:
- 3-sulfolactaldehyde reductase
- Sulfofructose kinase
- Sulfoquinovose isomerase
- Uncharacterized protein YihR
- Sulfoquinovosidase
- HTH-type transcriptional repressor CsqR
- Putative 2,3-dihydroxypropane-1-sulfonate exporter
- Putative sulfoquinovose importer
- 1-phosphofructokinase
- ATP-dependent 6-phosphofructokinase isozyme 2
Sequence:
MNKYTINDITRASGGFAMLAVDQREAMRMMFAAAGAPAPVADSVLTDFKVNAAKALSPYASAILVDQQFCYRQVVEQNAIAKSCAMIVAADEFIPGNGIPVDSVVIDRKINPLQIKQDGGKALKLLVLWRSDEDAQQRLDMVKEFNELCHSHGLVSIIEPVVRPPRRGDKFDREQAIIDAAKELGDSGADLYKVEMPLYGKGPQQELLCASQRLNDHINMPWVILSSGVDEKLFPRAVRVAMTAGASGFLAGRAVWASVVGLPDNELMLRDVCAPKLQQLGDIVDEMMAKRR
Protein: Dimethylallylcistransferase CPT1, chloroplastic (EC 2.5.1.28) (Cis-prenyltransferase 1) (SlCPT1) (Neryl-diphosphate synthase 1) (C1K5M2)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Function: Uses dimethylallyl diphosphate and isopentenyl diphosphate to catalyze the cis-prenyl chain elongation and produce the 10 carbon product neryl diphosphate.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:23134568}.
Interaction partners:
- ditrans,polycis-polyprenyl diphosphate synthase [
- Beta-phellandrene synthase
- isopentenyl-diphosphate Delta-isomerase
- (R)-linalool synthase TPS5, chloroplastic (Monoterpene synthase 1) (LeMTS1) (Terpenoid synthase 5)
Sequence:
MSSLVLQCWKLSSPSLILQQNTSISMGAFKGIHKLQIPNSPLTVSARGLNKISCSLNLQTEKLCYEDNDNDLDEELMPKHIALIMDGNRRWAKDKGLEVYEGHKHIIPKLKEICDISSKLGIQIITAFAFSTENWKRSKEEVDFLLQMFEEIYDEFSRSGVRVSIIGCKSDLPMTLQKCIALTEETTKGNKGLHLVIALNYGGYYDILQATKSIVNKAMNGLLDVEDINKNLFDQELESKCPNPDLLIRTGGEQRVSNFLLWQLAYTEFYFTNTLFPDFGEEDLKEAIMNFQQRHRRFGGHTY
Protein: Transcription factor Sp7 (C22) (Zinc finger protein osterix) (Q8VI67)
Organism: Mus musculus (Mouse)
Function: Transcriptional activator essential for osteoblast differentiation. Binds to SP1 and EKLF consensus sequences and to other G/C-rich sequences.
Subcellular location: Nucleus {ECO:0000269|PubMed:11792318}.
Interaction partners:
- Runt-related transcription factor 2
- Nuclear factor of activated T-cells, cytoplasmic 1
- Ribosomal oxygenase 1
- Osteocalcin
- Osteocalcin-2
- Osteocalcin-related protein
- Integrin-binding sialoprotein
- Sclerostin
- Osteopontin
- Homeobox protein DLX-5
Sequence:
MASSLLEEEAHYGSSPLAMLTAACSKFGGSSPLRDSTTLGKGGTKKPYADLSAPKTMGDAYPAPFSSTNGLLSPAGSPPAPASGYANDYPPFPHSFPGPTGAQDPGLLVPKGHSSSDCLPSVYTSLDMTHPYGSWYKAGIHAGISPGPGNTPTPWWDMHPGGNWLGGGQGQGDGLQGTLSTGPAQPPLNPQLPTYPSDFAPLNPAPYPAPHLLQPGPQHVLPQDVYKPKAVGNSGQLEGSGAAKPPRGAGTGGSGGYAGSGAGRSTCDCPNCQELERLGAAAAGLRKKPIHSCHIPGCGKVYGKASHLKAHLRWHTGERPFVCNWLFCGKRFTRSDELERHVRTHTREKKFTCLLCSKRFTRSDHLSKHQRTHGEPGPGPPPSGPKELGEGRSVGEEEANQPPRSSTSPAPPEKAHGGSPEQSNLLEI
Protein: LOC401296 protein (A2RU56)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDWGGGSTLTPAGASAQEPRLAQPSLGRPIPRVPHPVSVSTDQGLPDTCSGVAMGTSGRVSVAHTAVCRHTEGMHACVCAHLHVFTRTGHRRRCSHSGVHRPLCRCAHTQQGYVHRRVCVLAPGSGSRPTPHIVYSVPAARTCLGAPGSLSPCHLCVHICAHTYSGTPVCVHGCPGTLGSPSPRLPRLLESGTF
Protein: Proopiomelanocortin (Q7ZT12)
Organism: Ictalurus punctatus (Channel catfish) (Silurus punctatus)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Melanocyte-stimulating hormone receptor
- Melanocortin receptor 4-like.
- Melanocortin receptor 3
- Melanocortin receptor 5
- Melanocortin receptor 5
- Proenkephalin-B
- Proenkephalin a
- Proenkephalin b
- Opioid receptor, delta 1a
- Mu-type opioid receptor
Sequence:
MVKEARMGCPVWMLALALLCASGSEVRAQCWENSGCRDLSSDRNILECIRLCRSELTAESPLYPGDGHLQSVLLIPSEITTARLSTPQEDEAPESGPQHEEKRSYSMEHFRWGKPVGRKRRPIKVYANGVEEESSEALPAEMRRELGAVEDSTVSQQEKKDGSYKMNHFRWSGPPTSKRYGGFMKSWDEHSQKPLLTLFKNIINKDGHQKDH
Protein: Layilin (Q9Z209)
Organism: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Function: Receptor for hyaluronate.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Colocalizes with TLN1 at the membrane ruffles. {ECO:0000269|PubMed:9786953}.
Interaction partners:
Sequence:
MQPGPALQAVLLAVLLSEPRSSKGRLLSGQLVCRGGTRRPCYKVIYFHDAFQRLNFEEAKEACRRDGGQLVSIETEDEQRLIEKFIENLLASDGDFWIGLRRLEVKQVNNTACQDLYAWTDGSTSQFRNWYVDEPSCGSEVCVVMYHQPSAPPGIGGSYMFQWNDDRCNMKNNFICKYADEKPSTTPSIRPGGEATEPPTPVLPEETQKEDTKETFKESREAALNLAYILIPSIPLFLLLVVTSAACWVWICRRRKQEQPDPTTKEQHTIWPTPHQENSPNLDVYNVIRKQSEADLTEPRPDLKNISFRVCSSEAPPDDISCDYDNMAVNPSESGFVTLASMESGFVTNDIYEFSPDRMGRSKESGWVENEIYY
Protein: Serine/threonine-protein phosphatase (EC 3.1.3.16) (Q585J4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Protein phosphatase 2C, putative
- Phosphotyrosine protein phosphatase I domain-containing protein
Sequence:
MSTIVRKRGRTNSSEAQSGRWSHGARPDPSNRDRETIQRLVESILKDWQSAQELLDGQIISTILRLVRPILMAQPMLVRLQAPINVCGDIHGQIGDLVEIFRAGGMPPATNYLFLGDYVDRGKHGTEVIVVLLGLKILYPDGMCVLRGNHESDSICRIYGFFDEVKRRFSVKLFKEFTDVFNCLPIAALIDDIALCMHGGLSPDLRNLRQIERIERPLIVPDTGLACDLLWADPEEAGSGWMESERGVSYTFGEDIVKETCERLDIDVVLRAHQVVDKGYQFFAGRQLVTIFSASNYCGEFTNSGAMMIMDENCKCRFEIFRPQYD
Protein: Choline transporter-like protein (Q38AT3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU368066}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU368066}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MNKQYGTETNRYDYDVWQENQRNCRQECSPQAVPLQGIPLYQGDGDDKEELKRFVVQGYKDVWAAILYILCILATIGLGIYNIVKPDASGEEEEESVVSVKSSNPFSGVFKSVYIWIAVAGGIAIAVASLSFLFMRMFPRKIIIVANVVSIIINIGGAAAAIVMGVLPLGIALLIMCAMHILWFYFARHRIPFAAELLKASIDVLSGYKAVYLFNVMLCVGCAGFTILWGYAAVPSLETASNKGDSGALAVLLLLFLMLVFFWSSQVTGNLMHVTTAGLTATWYFAGKENMPKNPTLASFKRGTTTSFGSICFGSLLVAIIRLIRWLVSTAEGSEHEILRCIFLCIIGCLESLMEYFNTYAFVHVAIYGCGYIEAAKMTWELCKQCVFSALFNDTLIDVTLNLLVTCGSLLVGSVVGLLFRSWVAFALGFAVSILVHLLIFSPVTSAVTTLFVCYAEVPEGLEHSSPDLYAALQRTDQNGTSNGAAPPRV
Protein: CEP295 N-terminal-like protein (Differential display clone 8) (KIAA1731 N-terminal like protein) (Q497N6)
Organism: Mus musculus (Mouse)
Subcellular location: Cell projection, cilium {ECO:0000269|PubMed:19706271}. Note=Colocalizes to the motile cilium of mature spermatozoa.
Interaction partners:
Sequence:
MQRDTERAAQLSPSSEDEALVLRQKPLEMPAQEEDSTTLQQWKARQLQRLAEELKAEWQEARLQQVRQAERLYLSHLLDEAAERSMGNDPSVHEQNQRRTAKHTRAKERNRAAFREERGRREEHPRQHPKSRKKAPCSERRSSAKARGPASGEKGKRRRVSSSKDHDGYQGPRVTRRVGVAKLNPFFDGDTDCMEDVQKEFFREGRRPSAKGTHNLRDQSLQGKTTALTQPLLHGPTCKQEAAAQEPPSKYNKNLWHKEIESTFEELFNMNRKLKKHLNLHLEQRLKADQNPDEQQSYSEIRSETFGTPREERTEEVETAEESGSPTEVETTEMWSKVNLKQILSDSEYPRYQQIAKYPLKSESLVPVKAGTSREQDDLLSLSPESGQEPPKSPLLEDESLKPYLQKQADSVASWMALRQKQKAELEQRRQKALLELTEHPNMSLEIHYKAELEEERRARRRMRLALLKSNSTGICALPPDRNNLSLDNGLLDEDKQNQMIRDLQQQILEQNKLHQEFLEKARKRLQEFQKSF
Protein: UV excision repair protein RAD23 homolog A (HR23A) (hHR23A) (P54725)
Organism: Homo sapiens (Human)
Function: Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to 'Lys-48'-linked polyubiquitin chains in a length-dependent manner and with a lower affinity to 'Lys-63'-linked polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome.
Subcellular location: Nucleus.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 4
- Ataxin-3
- Polyubiquitin-C
- DNA repair protein complementing XP-C cells
- Centrin-2
- Ubiquitin-ribosomal protein eL40 fusion protein
- Polyubiquitin-B
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-protein ligase E3A
- Peptide-N
Sequence:
MAVTITLKTLQQQTFKIRMEPDETVKVLKEKIEAEKGRDAFPVAGQKLIYAGKILSDDVPIRDYRIDEKNFVVVMVTKTKAGQGTSAPPEASPTAAPESSTSFPPAPTSGMSHPPPAAREDKSPSEESAPTTSPESVSGSVPSSGSSGREEDAASTLVTGSEYETMLTEIMSMGYERERVVAALRASYNNPHRAVEYLLTGIPGSPEPEHGSVQESQVSEQPATEAAGENPLEFLRDQPQFQNMRQVIQQNPALLPALLQQLGQENPQLLQQISRHQEQFIQMLNEPPGELADISDVEGEVGAIGEEAPQMNYIQVTPQEKEAIERLKALGFPESLVIQAYFACEKNENLAANFLLSQNFDDE
Protein: Rab3 interacting molecule, isoform U (Rab3 interacting molecule, isoform X) (A0A0B4K7E1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Synapse {ECO:0000256|ARBA:ARBA00034103}.
Interaction partners:
Sequence:
MDEMPDLSHLTPHERMQIENVLMRQKQEEEKQNEIMRRKQDEVVTLEMQIRQRSEQQKKAGVELDATCHICLKTKFADGVGHICHYCNIRCCARCGGKVTLRSNKVIWVCILCRKKQELLSKTGQWINKTAAQQDGFIRRIEPDGSSDISQHPIVDPHDTTDKRPKLERTRSAAEKENLPMQRAGSMLRRQYSQQEQPTNRRLSASDSGMDPVMSPGQQMQHHQQQQRARMQPMNPQQAQQGYGMQQQQQPRSGGAYPDDDPRYYQGELDGLMRQHPHLAHPSQVQPQHTPQSHSQQQQSQHQQQHLMPQQHRPSPQQHSQQQQQQQQHSQQFAARQQQHQQQQHQQQVQQSYHAQIHQQPQQHPHPHSQQQQHHQQMQHQHGQSVPQMGGYQKPPPLTRNLTISGGHAMDSSAYSQQQQQQQRRALAGSQYASQQQRSFSSSEEEFQHQLLAAQGAVTVTAGSDYDGGRLQVRTSLDPWRQQRSLNERDLLSSGGGGGGGVGGADFRHLSHATQRLYASADQRDRYELQLQHRERLEQYPLTRTARLDVQQRNSLNRSNHERQFSGGGAGVGPGGAGGGGAAGAYRRAPPLAAAGGGGSSSSSTTSSSYYPQSKPQIVIGPGSGYDRGSGSMASMASAAAATAADAQGQAARNSQRGGLLGATRGGGGSSSVSSTEAAYWDEPATSSSSSAAQDSRRFTERRIKKTVRFDAHDEEASILASSSLPPVTAILPSTAVDVGAATILSSGKSLDAVGVGGADWSRWEAERQGSQDSATKDSGIDTSSTFTSSEDSNRGDGPKNPVNWQTSADNTRLIGHMILRKYYDGEDILGLKVNGGQPLATGGSVSGAGTGAAIGAGGPCGAIVEKVKRGSVADLEGRIRPGDEILEWNGRGLHNKSADEVYDIIDESRLDAQVELIVSRPIGSGGGSGGSSANVSPISGASGGSANSVPARRSSANFPHSGLASSMAGSAVVSSGGRYLQRKAPAVEAIEIHRDKPSVLITSPGSPDIHTSVSGPGSVSGSGLRQRGGVGQTQRLGPSHSTHSHSSSGSGSGSGSSTSSVHAPASAHGPVHASASASGSAPGGLHGTTTAGHHHHPHPHHYHPHQHPLPHPHQHQGPPAAHLQGHGVGGGIGMGSGSGTTTQPIPIEGRLQLKLGYDQNTLQLIVTLVCATGLSLRQSGAGRNPYAKVFLLPDRSHKSKRRTKTVGTTCEPRWGQTFVYSGLRRCDLNGRLLEVTLWDYVRYGANDFIGEVVIDLAHHILDDEAEWYQLQPHQDTSYLLRDEGSDVDGLILTPTDHLSPPSTMSRLSDSDTTSDCDIDGMTPGASISSMGSSASPPPLLELDLNERRSRRDMSPQGRKRVAGMVARDYRTVSGIGQSYHNQASATGYYRRGGGNGVGSAIGPGGMSLSQRSHSAAPSDGYHSSGVGGAASGGPAYGYRSTSPRRGSLSPPDDRYIDYPVLPVHGSSPNAPSVYQGPGGVSSAAASASQQQRFQSRSATATPTGSPKKRQLPQVPQTSRSAMLRDRLGQDFDERLASGGRFGRHRTRQPHHQATYRSTGMGGWERHYTGLSDSDLHSMDARMRPRHSLSPDKDFMGEFGDSDMESVVSVTSSAFSTQSERPRTSRGLSEYDKDKNGAEEAGGSKSAEGAGAEDKVDGSLSDTANDRKKGGGVDQERSPKGGSGMGKKSNSTSQLSATEQEQYQAQFAIAGSSTSSAGHHHITLPPPHPYHQRQSRGSAGSIQRSVEVPPVPPVTRYSAGSIHSITSSEGSSFSPSLRNDGALNEFVDGLGPGQLVGRQVLGAPSLGDIQLSLCHQKGCLEVEVIRARGLQQKAQSKMLPAPYVKVYLVSGKRCVDKMKTSSARRTLDPLYQQQLVFKQSYTGCILQITVWGDYGRIEKKVFMGVAQIMLDDLNLSNIVIGWYKLFGTTSLVSCPTNIGLGSRRSSIASLDSLKL
Protein: Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A (EC 3.1.4.35) (EC 3.1.4.53) (cAMP and cGMP phosphodiesterase 11A) (Q8VID6)
Organism: Rattus norvegicus (Rat)
Function: Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides cAMP and cGMP. Catalyzes the hydrolysis of both cAMP and cGMP to 5'-AMP and 5'-GMP, respectively.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9HCR9}.
Interaction partners:
- Adenosine kinase
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Adenine phosphoribosyltransferase
- GTP:AMP phosphotransferase AK3, mitochondrial
- Guanylate kinase
- Deoxycytidine kinase
- Adenylosuccinate lyase
- Inosine triphosphate pyrophosphatase
- Hypoxanthine-guanine phosphoribosyltransferase
Sequence:
MAASRLDFGEVETFLDRHPELFEDYLMRKGKQELVDKWLQRHSSGQGASDLRPALAGASSLAQSSARGSTGIGGGAGPQGSANSHPASGGGESAGVPLSPSWASGSRGDGNLQRRASQKELRKSFARSKAIHVNRTYDEQVTSRAQEPLSSVRRRALLRKASSLPPTTAHILSALLESRVNLPQYPPTAIDYKCHLKKHNERQFFLELVKDISNDLDLTSLSYKILIFVCLMVDADRCSLFLVEGAAAGKKTLVSKFFDVHAGTPLLPCSTTENSNEVQVPWGKGIIGYVGEHGETVNIPDAYQDRRFNDEIDKLTGYKTKSLLCMPIRNSDGEIIGVAQAINKVPEGAPFTEDDEKVMQMYLPFCGIAISNAQLFAASRKEYERSRALLEVVNDLFEEQTDLEKIVKKIMHRAQTLLKCERCSVLLLEDIESPVVKFTKSFELMSPKCSADAENSFKESVEKSSYSDWLINNSIAELVASTGLPVNVSDAYQDPRFDAEADQISGFHIRSVLCVPIWNSNHQIIGVAQVLNRLDGKPFDDADQRLFEAFVIFCGLGINNTIMYDQVKKSWAKQSVALDVLSYHATCSKAEVDKFKAANIPLVSELAIDDIHFDDFSLDVDAMITAALRMFMELGMVQKFKIDYETLCRWLLTVRKNYRMVLYHNWRHAFNVCQLMFAMLTTAGFQEILTEVEILAVIVGCLCHDLDHRGTNNAFQAKSDSALAQLYGTSATLEHHHFNHAVMILQSEGHNIFANLSSKEYSDLMQLLKQSILATDLTLYFERRTEFFELVSKGAYDWSITSHRDVFRSMLMTACDLGAVTKPWEISRQVAELVTSEFFEQGDRERSELKLTPSAIFDRNRKDELPRLQLEWIDSICMPLYQALVKVNAKLKPMLDSVAANRRKWEELHQKRLQVSAASPVPSSPSPAVAGEDRL
Protein: Tropinone reductase II (Q6KF77)
Organism: Solanum tuberosum (Potato)
Interaction partners:
Sequence:
MAAGRWNLEGCTALVTGGSRGIGYGIVEELASLGASVYTCSRNQKELNECLTQWRSKGFKVEASVCDLSSRSEREEFIKNVANHFDGKLNILVNNAGIVIYKEAKDYTMEDYSLIMSINFEAAYHLSVLAHPLLKASQRGNVVFISSISGASALPYEAVYGATKGAMDQLTRCLAFEWAKDNIRVNGVAPGVIASSMVEMTIQDPEQKENLDKLIDRCALHRMGEPKELAAVVAFLCFPAASYVTGQIIYVDGGFMANGGF
Protein: Transcription initiation factor IIE subunit alpha (TFIIE-alpha) (Factor A 66 kDa subunit) (Transcription factor A large subunit) (P36100)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Recruits TFIIH to the initiation complex and stimulates the RNA polymerase II C-terminal domain kinase and DNA-dependent ATPase activities of TFIIH. Both TFIIH and TFIIE are required for promoter clearance by RNA polymerase (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Transcription initiation factor IIF subunit alpha
- DNA-directed RNA polymerase II subunit RPB1
- General transcription and DNA repair factor IIH subunit TFB5
- Serine/threonine-protein kinase KIN28
- Transcription initiation factor IIE subunit beta
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB/SSL2
- General transcription and DNA repair factor IIH subunit TFB1
- DNA-directed RNA polymerase II subunit RPB7
- General transcription and DNA repair factor IIH subunit TFB2
- General transcription and DNA repair factor IIH subunit SSL1
Sequence:
MDRPIDDIVKNLLKFVVRGFYGGSFVLVLDAILFHSVLAEDDLKQLLSINKTELGPLIARLRSDRLISIHKQREYPPNSKSVERVYYYVKYPHAIDAIKWKVHQVVQRLKDDLDKNSEPNGYMCPICLTKYTQLEAVQLLNFDRTEFLCSLCDEPLVEDDSGKKNKEKQDKLNRLMDQIQPIIDSLKKIDDSRIEENTFEIALARLIPPQNQSHAAYTYNPKKGSTMFRPGDSAPLPNLMGTALGNDSSRRAGANSQATLHINITTASDEVAQRELQERQAEEKRKQNAVPEWHKQSTIGKTALGRLDNEEEFDPVVTASAMDSINPDNEPAQETSYQNNRTLTEQEMEERENEKTLNDYYAALAKKQAKLNKEEEEEEEEEEDEEEEEEEEMEDVMDDNDETARENALEDEFEDVTDTAGTAKTESNTSNDVKQESINDKTEDAVNATATASGPSANAKPNDGDDDDDDDDDEMDIEFEDV
Protein: APETALA2-like protein 1 (APETALA2-like protein 23) (Protein RICE STARCH REGULATOR 1) (Protein TARGET OF EAT 1) (OsTOE1) (Q2TQ34)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Probable transcription factor (By similarity). Involved in spikelet transition (Probable). Regulator of starch biosynthesis especially during seed development (e.g. endosperm starch granules); represses the expression of type I starch synthesis genes. Prevents lemma and palea elongation as well as grain growth.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00366}.
Interaction partners:
Sequence:
MELDLNNVAEGVVEKHETAARSDSGTSESSVLNGEASGAAIAPAEEGSSSTPPSPPPPPAAVLEFSILRSSASASGENDADDDEEEEATPSPPPHHQHQQLLVTRELFPSAAPSPQHWAELGFLRPDPPRPHPDIRILAHAPPPAPPPPPPQPQPQAAKKSRRGPRSRSSQYRGVTFYRRTGRWESHIWDCGKQVYLGGFDTAHAAARAYDRAAIKFRGVEADINFNLSDYEEDMRQMKSLSKEEFVHVLRRQSTGFSRGSSKYRGVTLHKCGRWEARMGQFLGKKYIYLGLFDSEVEAARAYDKAAIKCNGREAVTNFEPSTYDGELPTDAAAQGADVDLNLRISQPAASQQSPKRDSGSLGLQIHHGSFEGSEFKRAKNDAAPSELASRPHRFPLLTEHPPIWTAQPHPLFPNNEDASRSSDQKRKPSEGVAVPSWAWKQVSHHHPAPPHTLPLPFFSSSSSSPSSSSAAASSGFSKAATTAAAAQHTATLRFDPTAPSSSSSSRHHHHH
Protein: Protein FLX-like 3 (AtFLXL3) (Q9C717)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Has no transcriptional activation activity.
Interaction partners:
- Flowering time control protein FCA
- Flowering time control protein FPA
- Cleavage and polyadenylation specificity factor subunit 2
- Protein CTR9 homolog
- Protein FRIGIDA-ESSENTIAL 1
- FRIGIDA-like protein 1
Sequence:
MSGRNRIHRDIRDSYHDHRDLPPERPFLRGPPLLQPPPPSLLEDLQIQEGEIRRQDAEIRRLLSDNHGLADDRMVLERELVAAKEELHRMNLMISDLRAEQDLQLREFSEKRHKLEGDVRAMESYKKEASQLRGEVQKLDEIKRELSGNVQLLRKDLAKLQSDNKQIPGMRAEVKDLQKELMHARDAIEYEKKEKFELMEQRQTMEKNMVSMAREVEKLRAELATVDSRPWGFGGSYGMNYNNMDGTFRGSYGENDTYLGSSERSQYYSHGSGSQKKPRLDRH
Protein: Tuftelin-interacting protein 11 (Septin and tuftelin-interacting protein 1) (STIP-1) (Q9UBB9)
Organism: Homo sapiens (Human)
Function: Involved in pre-mRNA splicing, specifically in spliceosome disassembly during late-stage splicing events. Intron turnover seems to proceed through reactions in two lariat-intron associated complexes termed Intron Large (IL) and Intron Small (IS). In cooperation with DHX15 seems to mediate the transition of the U2, U5 and U6 snRNP-containing IL complex to the snRNP-free IS complex leading to efficient debranching and turnover of excised introns. May play a role in the differentiation of ameloblasts and odontoblasts or in the forming of the enamel extracellular matrix.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=In the nucleus localizes to unique speckle domains in close proximity to nuclear speckles and not identical to paraspeckles. {ECO:0000250}.
Interaction partners:
- ATP-dependent RNA helicase DHX15
- 116 kDa U5 small nuclear ribonucleoprotein component
- Crooked neck-like protein 1
- Tuftelin
- Pre-mRNA-processing factor 17
- U2 small nuclear ribonucleoprotein A'
- Intron Large complex component GCFC2
- Protein BUD31 homolog
- Pre-mRNA-splicing factor SYF1
- Pre-mRNA-processing-splicing factor 8
Sequence:
MSLSHLYRDGEGRIDDDDDERENFEITDWDLQNEFNPNRQRHWQTKEEATYGVWAERDSDDERPSFGGKRARDYSAPVNFISAGLKKGAAEEAELEDSDDEEKPVKQDDFPKDFGPRKLKTGGNFKPSQKGFAGGTKSFMDFGSWERHTKGIGQKLLQKMGYVPGRGLGKNAQGIINPIEAKQRKGKGAVGAYGSERTTQSMQDFPVVDSEEEAEEEFQKELSQWRKDPSGSKKKPKYSYKTVEELKAKGRISKKLTAPQKELSQVKVIDMTGREQKVYYSYSQISHKHNVPDDGLPLQSQQLPQSGKEAKAPGFALPELEHNLQLLIDLTEQEIIQNDRQLQYERDMVVNLFHELEKMTEVLDHEERVISNLSKVLEMVEECERRMQPDCSNPLTLDECARIFETLQDKYYEEYRMSDRVDLAVAIVYPLMKEYFKEWDPLKDCTYGTEIISKWKSLLENDQLLSHGGQDLSADAFHRLIWEVWMPFVRNIVTQWQPRNCDPMVDFLDSWVHIIPVWILDNILDQLIFPKLQKEVENWNPLTDTVPIHSWIHPWLPLMQARLEPLYSPIRSKLSSALQKWHPSDSSAKLILQPWKDVFTPGSWEAFMVKNIVPKLGMCLGELVINPHQQHMDAFYWVIDWEGMISVSSLVGLLEKHFFPKWLQVLCSWLSNSPNYEEITKWYLGWKSMFSDQVLAHPSVKDKFNEALDIMNRAVSSNVGAYMQPGARENIAYLTHTERRKDFQYEAMQERREAENMAQRGIGVAASSVPMNFKDLIETKAEEHNIVFMPVIGKRHEGKQLYTFGRIVIYIDRGVVFVQGEKTWVPTSLQSLIDMAK
Protein: Rho guanine nucleotide exchange factor 12 (Leukemia-associated RhoGEF) (Q9NZN5)
Organism: Homo sapiens (Human)
Function: May play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase and may act as GTPase-activating protein (GAP) for GNA12 and GNA13.
Subcellular location: Cytoplasm {ECO:0000305}. Membrane {ECO:0000305}. Note=Translocated to the membrane upon stimulation. {ECO:0000305}.
Interaction partners:
- Transforming protein RhoA
- Guanine nucleotide-binding protein subunit alpha-12
- Guanine nucleotide-binding protein subunit alpha-13
- Plexin-B1
- Plexin-B2
- Guanine nucleotide-binding protein G
- CD44 antigen
- Plexin-B3
- Rho guanine nucleotide exchange factor 11
- Rho guanine nucleotide exchange factor 7
Sequence:
MSGTQSTITDRFPLKKPIRHGSILNRESPTDKKQKVERIASHDFDPTDSSSKKTKSSSEESRSEIYGLVQRCVIIQKDDNGFGLTVSGDNPVFVQSVKEDGAAMRAGVQTGDRIIKVNGTLVTHSNHLEVVKLIKSGSYVALTVQGRPPGSPQIPLADSEVEPSVIGHMSPIMTSPHSPGASGNMERITSPVLMGEENNVVHNQKVEILRKMLQKEQERLQLLQEDYNRTPAQRLLKEIQEAKKHIPQLQEQLSKATGSAQDGAVVTPSRPLGDTLTVSEAETDPGDVLGRTDCSSGDASRPSSDNADSPKSGPKERIYLEENPEKSETIQDTDTQSLVGSPSTRIAPHIIGAEDDDFGTEHEQINGQCSCFQSIELLKSRPAHLAVFLHHVVSQFDPATLLCYLYSDLYKHTNSKETRRIFLEFHQFFLDRSAHLKVSVPDEMSADLEKRRPELIPEDLHRHYIQTMQERVHPEVQRHLEDFRQKRSMGLTLAESELTKLDAERDKDRLTLEKERTCAEQIVAKIEEVLMTAQAVEEDKSSTMQYVILMYMKHLGVKVKEPRNLEHKRGRIGFLPKIKQSMKKDKEGEEKGKRRGFPSILGPPRRPSRHDNSAIGRAMELQKARHPKHLSTPSSVSPEPQDSAKLRQSGLANEGTDAGYLPANSMSSVASGASFSQEGGKENDTGSKQVGETSAPGDTLDGTPRTLNTVFDFPPPPLDQVQEEECEVERVTEHGTPKPFRKFDSVAFGESQSEDEQFENDLETDPPNWQQLVSREVLLGLKPCEIKRQEVINELFYTERAHVRTLKVLDQVFYQRVSREGILSPSELRKIFSNLEDILQLHIGLNEQMKAVRKRNETSVIDQIGEDLLTWFSGPGEEKLKHAAATFCSNQPFALEMIKSRQKKDSRFQTFVQDAESNPLCRRLQLKDIIPTQMQRLTKYPLLLDNIAKYTEWPTEREKVKKAADHCRQILNYVNQAVKEAENKQRLEDYQRRLDTSSLKLSEYPNVEELRNLDLTKRKMIHEGPLVWKVNRDKTIDLYTLLLEDILVLLQKQDDRLVLRCHSKILASTADSKHTFSPVIKLSTVLVRQVATDNKALFVISMSDNGAQIYELVAQTVSEKTVWQDLICRMAASVKEQSTKPIPLPQSTPGEGDNDEEDPSKLKEEQHGISVTGLQSPDRDLGLESTLISSKPQSHSLSTSGKSEVRDLFVAERQFAKEQHTDGTLKEVGEDYQIAIPDSHLPVSEERWALDALRNLGLLKQLLVQQLGLTEKSVQEDWQHFPRYRTASQGPQTDSVIQNSENIKAYHSGEGHMPFRTGTGDIATCYSPRTSTESFAPRDSVGLAPQDSQASNILVMDHMIMTPEMPTMEPEGGLDDSGEHFFDAREAHSDENPSEGDGAVNKEEKDVNLRISGNYLILDGYDPVQESSTDEEVASSLTLQPMTGIPAVESTHQQQHSPQNTHSDGAISPFTPEFLVQQRWGAMEYSCFEIQSPSSCADSQSQIMEYIHKIEADLEHLKKVEESYTILCQRLAGSALTDKHSDKS