wanglab/gogpt-training-data huggingface dataset:
Protein: Phosphate transporter PHO1 (Protein PHO1) (AtPHO1) (Q8S403)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Inositol polyphosphate sensor that associates with transcription factors to regulate inorganic phosphate (Pi) starvation responses. Probably acts by binding inositol polyphosphate via its SPX domain. Acts as a Pi exporter, mediating efflux of Pi out of cells. Transfers Pi from the epidermal and cortical cells to the root xylem vessels. Involved in the transfer of Pi from roots to shoots. Involved in abscisic acid (ABA) induction of stomatal closure and ABA repression of stomatal opening.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:22449068, ECO:0000269|PubMed:22634761, ECO:0000269|PubMed:26546667}; Multi-pass membrane protein {ECO:0000305}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:22449068, ECO:0000269|PubMed:26546667}; Multi-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:22634761}; Multi-pass membrane protein {ECO:0000305}. Note=In transgenic plants, relocates partially to the plasma membrane in the presence of high extracellular Pi. {ECO:0000269|PubMed:22449068}.
Interaction partners:
- Probable ubiquitin-conjugating enzyme E2 24
- Inorganic phosphate transporter 1-1
- Inositol-3-phosphate synthase isozyme 1
- Protein PHOSPHATE STARVATION RESPONSE 1
- Inorganic phosphate transporter 1-4
- SPX domain-containing protein 1
- Probable inorganic phosphate transporter 1-5
- Leucine-rich repeat receptor protein kinase EMS1
- WRKY transcription factor 6
- E3 SUMO-protein ligase SIZ1
Sequence:
MVKFSKELEAQLIPEWKEAFVNYCLLKKQIKKIKTSRKPKPASHYPIGHHSDFGRSLFDPVRKLARTFSDKLFSNSEKPEILQVRRRRGSSETGDDVDEIYQTELVQLFSEEDEVKVFFARLDEELNKVNQFHKPKETEFLERGEILKKQLETLAELKQILSDRKKRNLSGSNSHRSFSSSVRNSDFSAGSPGELSEIQSETSRTDEIIEALERNGVSFINSATRSKTKGGKPKMSLRVDIPDAVAGAEGGIARSIATAMSVLWEELVNNPRSDFTNWKNIQSAEKKIRSAFVELYRGLGLLKTYSSLNMIAFTKIMKKFDKVAGQNASSTYLKVVKRSQFISSDKVVRLMDEVESIFTKHFANNDRKKAMKFLKPHQTKDSHMVTFFVGLFTGCFISLFVIYIILAHLSGIFTSSDQVSYLETVYPVFSVFALLSLHMFMYGCNLYMWKNTRINYTFIFEFAPNTALRYRDAFLMGTTFMTSVVAAMVIHLILRASGFSASQVDTIPGILLLIFICVLICPFNTFYRPTRFCFIRILRKIVCSPFYKVLMVDFFMGDQLTSQIPLLRHLETTGCYFLAQSFKTHEYNTCKNGRYYREFAYLISFLPYFWRAMQCVRRWWDESNPDHLINMGKYVSAMVAAGVRITYARENNDLWLTMVLVSSVVATIYQLYWDFVKDWGLLNPKSKNPWLRDNLVLRNKNFYYLSIALNLVLRVAWIETIMRFRVSPVQSHLLDFFLASLEVIRRGHWNFYRVENEHLNNVGQFRAVKTVPLPFLDRDSDG
Protein: Cyclic AMP-dependent transcription factor ATF-2 (B8ZZU6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR003153}.
Interaction partners:
Sequence:
MSDDKPFLCTAPGCGQRFTNEDHLAVHKHKHEMTLKFGPARNDSVIVADQTPTPTRFLKNCEEVGLFNELASPFENEFKKASEDDIKKMPLDLSPLATPIIRSKIEEPSVVETTHQDSPLPHPESTTSDEKLVRPVTMVPSVPGIPGPSSPQPVQSEAKMRLKAALTQQHPPVTNGDTVKGHGSGLVRTQSEESRPQSLQQPATSTTETPASPAHTTPQTQSTSGRRRRAANEDPDEKRRKFLERNRAAASRCRQKRKVWVQSLEKKAEDLSSLNGQLQSEVTLLRNEVAQLKQLLLAHKDCPVTAMQKKSGYHTADKDDSSEDISVPSSPHTEAIQHSSVSTSNGVSSTSKAEAVATSVLTQMADQSTEPALSQIVMAPSSQSQPSGS
Protein: ATP-dependent DNA helicase PIF5 (EC 3.6.4.12) (DNA repair and recombination helicase PIF5) (Q580X6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Function: DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of mitochondrial (kinetoplast) genome stability. Involved in processing of minicircle Okazaki fragments.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:19646907, ECO:0000269|PubMed:19779567}. Note=Enriched in the antipodal sites flanking the kDNA disk.
Interaction partners:
- DNA polymerase
- Mitochondrial DNA polymerase beta-PAK
- TFIIH basal transcription factor complex helicase/translocase XPB subunit
Sequence:
MLSRLSAVWRPSRVALRIQRVDFTTCGNRLNRSTQPNEPPLVSGIAARSRTAKAEPVEKRGRAAIKIDSPPPPLEPPRISEEHMTRRRKVGGGKTKAAAVTKSKQRRSGRTVGASAFNTARRANGIEGSAPGKGGASDVAIDDDDDEKLVDEESKQLMQLLKEEALRREEEKKKRLRAKAAAEPTEVTDDKEYLSKLGVAERTQPVGTEAKISAQGKAEGASEGQTHFSDADADSQLPILTSLSPEQQRALRLALKGRNLFITGGAGSGKSLLIREIVYQLRHNKRRCVYVTATTGVAALNVRGSTVNSFAGVKFGDGDARQLLKWVRRSRRAAGRWRYCQTLIIDEISMMDPLLLDKLDVIARAIRRRNEPFGGIQVILCGDFLQLPPIPPRNKPQQKTEENAEAQEGGDPTDGTPAPSKLQYCFETSTWTSLNLITVILHKKFRQHDDLAFQQVLDELRVGSLSPESYELLLSRTVASKSSAKSRKKKDEDAGNDGVLPLTDAETTPAAAEKDRHVRLCATNKEVEMRNAKYFAALEPKGLPIYPSPNDGSSQQTGSSNGANSVTEEDTMRPLQVYRAYDAYSTHETEPETTEETTTGTQPSQPWVRFEDSTLPTDLALKVGTRVMVLQNISLRLGLVNGSVGEVVGFLHPLELVELVLRAPRERHFPSARGQELLERAGLPTLQDAFRCVDTALGQSLFYYLRERGIRRPEDASYGCVYGNTHCRDILRLVGLGKTESANAVHPLEMYLGGIAPQHVRLTRLPIVRLDLREGNHTSSDSGAVEDGGFANGSKRLPKHVYAFISPSSHQWYMGDQPVATRTQLPLRQAWAMTVHKAQGLTISHVEVAIHRFFSPGQAYVALSRSTRLDNIRLLDFNNASVHACPRAKEFYTVLEEEELDNEIEDDGTEGDEEALEGDGEYEGEVEE
Protein: Putative glycine dehydrogenase (decarboxylating), mitochondrial (EC 1.4.4.2) (Glycine cleavage system P protein) (Glycine decarboxylase) (Glycine dehydrogenase (aminomethyl-transferring)) (Q09785)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable aminomethyltransferase, mitochondrial
- Putative glycine cleavage system H protein, mitochondrial
- Serine hydroxymethyltransferase, mitochondrial
- Probable serine hydroxymethyltransferase, cytosolic
- Probable low-specificity L-threonine aldolase
- Dihydrolipoyl dehydrogenase, mitochondrial
- Glutamate synthase
- Glutamine synthetase
- DASH complex subunit dad4
- D-amino-acid oxidase
Sequence:
MFDSFMKRNQLALIMFRACSKLQYHGVNTSLSRHLFLAKRNLSISSACLEAKNSQKFPALDTFEPRHIGPSKTDQQYQLESLGYKDFDSFLKDVIPDSVRTPESQLMAFGSVNPNEKNPPVNYSESEFTTLANNVANQNKLIKSFIGMGYYNVKLPAAIQRNVLENPEWYTQYTPYQAEISQGRLESMMNYQTMIADLTGLSISNASLLDEGTAAGEAMVMLMANDKKKRKTFLVDKNIYPNTLSVLRTRASGFGIKIELDNITPELITKSAKHVFGIFVQYPAADGSIFDYGHLAATARSFNMHVVAATDLLALTILKSPGEWGADVAVGSTQRFGLPMGYGGPHAGFFACSEEFKRKIPGRLIGLSKDRLENPAYRLALQTREQHIRREKATSNICTAQALLANMSAFYAIYHGPNGLQEIANRIYASTSFLKSALESSGYKIVNKSHFFDTLTIEVESADKVLAKALDHGYNLRKVDDSHVGLSLDETVCDKDIQALFSIFNINKSVDQYYMEIATSEPNGNSASTVDNLSICSLPENFRRTTLYLQHPVFNRYHSETELMRYIHHLQSKDLSLAHAMTPLGSCTMKLNAVTEMMPITNPLFANIHPYVPEEQAKGYRHVIEDLQLMLTTITGFDAACFQPNSGAAGEYTGLSVIRAYQRSIGQGHRNICLIPVSAHGTNPASAAMAGFTVIPVKCLNNGYLDMQDLKEKASKHADKLAAFMVTYPSTFGIFEPDVKEALEVIHEHGGQVYFDGANMNAMVGLCKAGDIGADVCHLNLHKTFCIPHGGGGPGVGPICVKKHLADFLPSHPVVSCGGKNGITSVSSSPFGSAGILPISWAYMRMMGLAGLRDASKAALLNANYMAKRLSSHYKLVYTNKNNLCAHEFILDAREFKATAGVDATDIAKRLQDYSFHAPTLSWPIANTLMIEPTESESMYEMDRFCDALISIRQEIREIEEGLQPKDNNLLVNAPHPQKDIASEKWDRPYTRERAVYPVPLLKERKFWPSVARLDDAYGDKNLFCTCSPVV
Protein: Aspartate aminotransferase (AspAT) (EC 2.6.1.1) (Transaminase A) (P00509)
Organism: Escherichia coli (strain K12)
Subcellular location: Cytoplasm.
Interaction partners:
- Malate dehydrogenase
- T-protein
- Bifunctional chorismate mutase/prephenate dehydratase
- NADP-specific glutamate dehydrogenase
- Histidinol-phosphate aminotransferase
- Isocitrate dehydrogenase
- L-asparaginase 1
- Glutamate-pyruvate aminotransferase AlaA
- Adenylosuccinate synthetase
- Argininosuccinate synthase
Sequence:
MFENITAAPADPILGLADLFRADERPGKINLGIGVYKDETGKTPVLTSVKKAEQYLLENETTKNYLGIDGIPEFGRCTQELLFGKGSALINDKRARTAQTPGGTGALRVAADFLAKNTSVKRVWVSNPSWPNHKSVFNSAGLEVREYAYYDAENHTLDFDALINSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQLSVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAAMHKELIVASSYSKNFGLYNERVGACTLVAADSETVDRAFSQMKAAIRANYSNPPAHGASVVATILSNDALRAIWEQELTDMRQRIQRMRQLFVNTLQEKGANRDFSFIIKQNGMFSFSGLTKEQVLRLREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL
Protein: Heat shock 70 kDa protein 4 (Heat shock 70-related protein APG-2) (Q61316)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- DnaJ homolog subfamily B member 1
- E3 ubiquitin-protein ligase CHIP
- Tight junction protein 1
- Heat shock cognate 71 kDa protein
- Heat shock 70 kDa protein 1B
- Heat shock protein HSP 90-alpha
- 60 kDa heat shock protein, mitochondrial
- BAG family molecular chaperone regulator 1
- Stress-70 protein, mitochondrial
- BAG family molecular chaperone regulator 3
Sequence:
MSVVGIDLGFQSCYVAVARAGGIETIANEYSDRCTPACVSFGPKNRSIGAAAKSQVISNAKNTVQGFKRFHGRAFSDPFVEAEKSNLAYDIVQLPTGLTGIKVTYMEEERNFTTEQVTAMLLSKLKETAESVLKKPVVDCVVSVPSFYTDAERRSVMDATQIAGLNCLRLMNETTAVALAYGIYKQDLPALEEKPRNVVFVDMGHSAYQVSVCAFNKGKLKVLATAFDTTLGGRKFDEVLVNHFCEEFGKKYKLDIKSKIRALLRLSQECEKLKKLMSANASDLPLSIECFMNDIDVSGTMNRGKFLEMCDDLLARVEPPLRSVLEQSKLKKEDIYAVEIVGGATRIPAVKEKISKFFGKELSTTLNADEAVTRGCALQCAILSPAFKVREFSITDVVPYPISLRWNSPAEEGLSDCEVFPKNHAAPFSKVLTFYRKEPFTLEAYYSSPQDLPYPDPAIAQFSVQKVTPQSDGSSSKVKVKVRVNVHGIFSVSSAALVEVHKSEESEEPMETDQNAKEEEKMQVDQEEPHTEEQQQQPQTPAENKAESEEMETSQAGSKDKKTDQPPQAKKAKVKTSTVDLPIEHTLWQLDREMLALYTENEGKMIMQDKLEKERNDAKNAVEEYVYEMRDKLSGEYEKFVSEDDRNTFTLKLEDTENWLYEDGEDQPKQVYVDKLAELKSLGQPIKTRFQESEERPKLFEELGKQIQQYMKVISSFKNKEDQYEHLDAADVTKVEKSTNEAMEWMNSKLNLQNKQSLTVDPVVKTKEIEAKIKELTSICSPIISKPKPKVEPPKEEPKHAEQNGPVDGQGDNPGSQAAEHGADTAVPSDGDKKLPEMDID
Protein: Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 1 (EC 1.8.1.-) (Q8WU10)
Organism: Homo sapiens (Human)
Function: Probable FAD-dependent oxidoreductase; involved in the cellular oxidative stress response. Required for normal sarcomere structure and muscle fiber integrity (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:27745833}. Cytoplasm {ECO:0000269|PubMed:27745833}. Cytoplasm, myofibril, sarcomere {ECO:0000269|PubMed:27745833}.
Interaction partners:
- Uracil phosphoribosyltransferase homolog
Sequence:
MEAARPPPTAGKFVVVGGGIAGVTCAEQLATHFPSEDILLVTASPVIKAVTNFKQISKILEEFDVEEQSSTMLGKRFPNIKVIESGVKQLKSEEHCIVTEDGNQHVYKKLCLCAGAKPKLICEGNPYVLGIRDTDSAQEFQKQLTKAKRIMIIGNGGIALELVYEIEGCEVIWAIKDKAIGNTFFDAGAAEFLTSKLIAEKSEAKIAHKRTRYTTEGRKKEARSKSKADNVGSALGPDWHEGLNLKGTKEFSHKIHLETMCEVKKIYLQDEFRILKKKSFTFPRDHKSVTADTEMWPVYVELTNEKIYGCDFIVSATGVTPNVEPFLHGNSFDLGEDGGLKVDDHMHTSLPDIYAAGDICTTSWQLSPVWQQMRLWTQARQMGWYAAKCMAAASSGDSIDMDFSFELFAHVTKFFNYKVVLLGKYNAQGLGSDHELMLRCTKGREYIKVVMQNGRMMGAVLIGETDLEETFENLILNQMNLSSYGEDLLDPNIDIEDYFD
Protein: Glycophorin-A (MN sialoglycoprotein) (PAS-2) (Sialoglycoprotein alpha) (CD antigen CD235a) (P02724)
Organism: Homo sapiens (Human)
Function: Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane. Is a receptor for influenza virus. Is a receptor for Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. Appears to be a receptor for Hepatitis A virus (HAV).
Subcellular location: Cell membrane {ECO:0000269|PubMed:11402026}; Single-pass type I membrane protein {ECO:0000269|PubMed:11402026}. Note=Appears to be colocalized with SLC4A1.
Interaction partners:
- Glycophorin-B
- Band 3 anion transport protein
- Ammonium transporter Rh type A
- Blood group Rh
- Ankyrin-1
- Protein 4.2
- Leukocyte surface antigen CD47
- Glycophorin-C
- Krueppel-like factor 1
- Outer mitochondrial transmembrane helix translocase
Sequence:
MYGKIIFVLLLSEIVSISALSTTEVAMHTSTSSSVTKSYISSQTNDTHKRDTYAATPRAHEVSEISVRTVYPPEEETGERVQLAHHFSEPEITLIIFGVMAGVIGTILLISYGIRRLIKKSPSDVKPLPSPDTDVPLSSVEIENPETSDQ
Protein: Nucleoid-associated protein SP_1102 (P67266)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Function: Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
Subcellular location: Cytoplasm, nucleoid {ECO:0000255|HAMAP-Rule:MF_00274}.
Interaction partners:
Sequence:
MMNMQNMMRQAQKLQKQMEQSQAELAAMQFVGKSAQDLVQATLTGDKKVVSIDFNPAVVDPEDLETLSDMTVQAINSALEQIDETTKKKLGAFAGKLPF
Protein: Potassium transporter 1 (OsHAK1) (Q6VVA6)
Organism: Oryza sativa subsp. japonica (Rice)
Function: High-affinity potassium transporter. Also transports rubidium, with the same affinity and cesium, with a lower affinity.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Os04g0589400 protein
Sequence:
MSSALEVEGSGSPGVEPAATATASRLKRHDSLFGDAEKVSGGKHHGGSAVSWAVTLHLAFQSVGIIYGDIGTSPLYVYSSTFPDGIGHRDDLVGVLSLILYTLIIIPMLKYVFIVLYANDNGDGGTFALYSLISRYAKIRMIPNQQAEDAMVSNYSIEAPSSQLRRAQWVKHKLESSRAAKMALFFLTILGTSMVMGDGTLTPAISVLSAVSGIREKAPNLTQTQVVLISVAILFMLFSVQRFGTDKVGYTFAPIISVWFLLIAGIGLYNLVVHEITILKAFNPWYIVQYFRRNGKKGWVSLGGVVLCVTGTEGMFADLGHFNIRAVQISFNCILFPSVALCYIGQAAYLRKFPENVSDTFYKSIPGKYRDRLNFGPLFWPTFIVAILAAIIASQAMLSGAFAILSKALSLGCLPRVRVIHTSKKYEGQVYIPEVNFMMGLASIIVTIAFRTTTSIGNAYGICVVTTFMVTTHLMTVVMLLIWKKHLVFILLFYCVFGFTEVVYLSSILSKFVDGGYLPFCFAMVLMTMMATWHYVHVRRYWYELDHIVPTAELASLLEENGGVRRVPGVGLLYTELVQGIPPLFPRLVRKIPSVHAVFVFISIKHLPIPHVAAAERFLFRQVGPRARRVFRCVARYGYTDALEEPREFAAFLVDGLKMFIQEESAFAPHQEMIDAAADDDDEAAARPRRSTSSAVHSEEAIQAASSGRTTASSVQLQAGGEPPAAMDVEEEKRLIDREVGRGVVYLMGEANVSAGPNSSILKRIAVNYIYTFLRKNLTEGHRALAIPNDQLLKVGITYEI
Protein: Acetylcholine receptor subunit alpha-type deg-3 (P54244)
Organism: Caenorhabditis elegans
Function: Subunit of the non-synaptic neuronal acetylcholine receptor, which may play a role in chemotaxis towards choline. After binding choline or acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Subcellular location: Postsynaptic cell membrane {ECO:0000269|PubMed:11273652}; Multi-pass membrane protein {ECO:0000269|PubMed:11273652}. Cell membrane {ECO:0000269|PubMed:11273652}; Multi-pass membrane protein {ECO:0000269|PubMed:11273652}. Note=Enriched in the sensory endings of sensory neurons.
Interaction partners:
- Resistance to inhibitors of cholinesterase protein 3
- Degenerin mec-4
- Degenerin deg-1
- Acetylcholine receptor subunit alpha-type des-2
Sequence:
MTLKIRTIIILFCVISVTTTSQSLNATLKTFDPRLLNSTADRDIAMKNVPLVRLTRHLLSPERYDVRVRPILDHKKSLKVHISISLYQIIEVDEPSQNIKLNVWMIQKWRDEYLDWNPNEYGMINSTIIPFHHLWIPDTYLYNSVKMSRDETERYMNIQATSNYWKGEKGAELSFLYPAIYTITCRLNIRFFPYDRQNCTLTISSWTNSKSALDYYADTEVSMQSFIPNEEWQVKSFKIHRHEYKYACCAEPWVILQASLVIQRKPLYYLVNLIIPTSIITLVAITGFFTPASTDDDRTEKINLGITTLLAMSILMLMVSDQMPTTSEFVPLIAWFYLSIIIIISIGTFLTSVVLSVQGRRQYGRNPPQFIRYIFFVLLPQVLLLNVPPPLQTLWGELDDDPLNVRRRKKSHYLSRNVNNGSTKMASPMSTLRVPQSAGSVSEKRQSFQMIDVTSPNSPNTARSRAPSLAPSTAKATMWEGTMSALAGTNTQLRRTSNVFNKEVDEMRRKRQCSLEWEFLATVLDRFLLIVFVGAVVIVTAGLILVGRMAQYSYDHPDDRFFNV
Protein: NERD domain-containing protein (Q38A54)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTHYVDSVLYWFPTLVLVVCMIVLIVTAVGLSLGKFWRGLSSWSWRRIFSLTRMSMRQTTFRASMNAEEAVETALRKAGWKHVFLRRRVFVPRLQHNREIDVVAVGPVVLVVEVKHWRGSVWCNGQRWFQQVHKTARALEFEDIREDNVVKAAALRRHIENDKRVPLPDFNLLSDCLQESEGDGTWYEDRRLHKQCGTVIIPVVVFTNPLVRLDPSTVKQKDDVFDLPGLERYARNLLYNTRGASVFDYYKQRVDEFLRPIFIGRSITPDTYCLSFFTEEKVARVVERMRTWDMVYLLNGRLVHGDIVSFGLPSTNRHFVRQQISDVEITWFDGLIGFARTMWMNSGGMVKITLSSPRKRKVFSFPLMPRHLKSIYKNDRLVLKLAGTTNLEEIPLADIATLRLSQHRETDGS
Protein: 6-phosphogluconolactonase 3 (6PGL) (EC 3.1.1.31) (P38858)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Glucose-6-phosphate 1-dehydrogenase
- 6-phosphogluconate dehydrogenase, decarboxylating 1
- 6-phosphogluconate dehydrogenase, decarboxylating 2
- Probable gluconokinase
- Exportin-T
- Transaldolase
- Transketolase 1
- Transketolase 2
- Ribulose-phosphate 3-epimerase
- Glucose-6-phosphate isomerase
Sequence:
MVTVGVFSERASLTHQLGEFIVKKQDEALQKKSDFKVSVSGGSLIDALYESLVADESLSSRVQWSKWQIYFSDERIVPLTDADSNYGAFKRAVLDKLPSTSQPNVYPMDESLIGSDAESNNKIAAEYERIVPQVLDLVLLGCGPDGHTCSLFPGETHRYLLNETTKRVAWCHDSPKPPSDRITFTLPVLKDAKALCFVAEGSSKQNIMHEIFDLKNDQLPTALVNKLFGEKTSWFVNEEAFGKVQTKTF
Protein: Ribosomal oxygenase 2 (Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA) (EC 1.14.11.79) (Histone lysine demethylase MINA) (MYC-induced nuclear antigen) (Q8CD15)
Organism: Mus musculus (Mouse)
Function: Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Is involved in the demethylation of trimethylated 'Lys-9' on histone H3 (H3K9me3), leading to an increase in ribosomal RNA expression. Also catalyzes the hydroxylation of 60S ribosomal protein L27a on 'His-39' (By similarity). May play an important role in cell growth and survival. May be involved in ribosome biogenesis, most likely during the assembly process of pre-ribosomal particles.
Subcellular location: Nucleus {ECO:0000269|PubMed:16533354}. Nucleus, nucleolus {ECO:0000269|PubMed:16533354}.
Interaction partners:
- Large ribosomal subunit protein uL2
- tRNA wybutosine-synthesizing protein 5
- Large ribosomal subunit protein uL15
- 2-oxoglutarate and iron-dependent oxygenase JMJD4
Sequence:
MPKKVQPTGDENEEASVPCKRVKEELPETLSVLNFDSPSSFFESLISPIKVETFFKEFWEQKPLLIQRDDPVLAKYYQSLFSLSDLKRLCKKGVYYGRDVNVCRSISGKKKVLNKDGRAHFLQLRKDFDQKRATIQFHQPQRYKDELWRIQEKLECYFGSLVGSNVYMTPAGSQGLPPHYDDVEVFILQLEGTKHWRLYSPTVPLAHEYSVESEDRIGTPTHDFLLKPGDLLYFPRGTIHQAETPSGLAYSIHLTISTYQNNSWGDCLLDSISGFVFDIAKEDVALRSGMPRRMLLNVETPADVTRKLSGFLRTLADQLEGREELLSSDMKKDFVKHRLPPFFEGNGTETMDPGKQLPRLDNIIRLQFKDHIVLTVGPDKNPFDEAQQKVVYIYHSLKNVRQMHMIGEEEESEIFGLRFPLSHVDALKQIWCGSPIRVKDLKLDTDEEKENLALSLWSESLIQVL
Protein: MICAL-like protein 1 (Molecule interacting with Rab13) (MIRab13) (Q8N3F8)
Organism: Homo sapiens (Human)
Function: Probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. On endosome membranes, may act as a downstream effector of Rab proteins recruiting cytosolic proteins to regulate membrane tubulation. May be involved in a late step of receptor-mediated endocytosis regulating for instance endocytosed-EGF receptor trafficking. Alternatively, may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. May indirectly play a role in neurite outgrowth.
Subcellular location: Recycling endosome membrane {ECO:0000269|PubMed:19864458, ECO:0000269|PubMed:21951725, ECO:0000269|PubMed:34100897}; Peripheral membrane protein {ECO:0000269|PubMed:19864458, ECO:0000269|PubMed:34100897}. Late endosome membrane. Cell projection, cilium membrane {ECO:0000269|PubMed:31615969}; Peripheral membrane protein {ECO:0000269|PubMed:31615969}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:31615969}. Note=Localization to late endosomes is actin-dependent. Association to tubular recycling endosomes is regulated by RAB35 and ARF6 (PubMed:21951725). Interaction with tubulins achors MICALL1 to the centriole (PubMed:31615969). {ECO:0000269|PubMed:21951725, ECO:0000269|PubMed:31615969}.
Interaction partners:
- EH domain-containing protein 1
- Ubiquitin-like protein FUBI
- Eukaryotic translation initiation factor 3 subunit E
- Eukaryotic translation initiation factor 3 subunit D
- EH domain-containing protein 3
- Ras-related protein Rab-8A
- Eukaryotic translation initiation factor 3 subunit K
- Protein kinase C and casein kinase substrate in neurons protein 2
- Eukaryotic translation initiation factor 3 subunit M
- Ras-related protein Rab-35
Sequence:
MAGPRGALLAWCRRQCEGYRGVEIRDLSSSFRDGLAFCAILHRHRPDLLDFDSLSKDNVFENNRLAFEVAEKELGIPALLDPNDMVSMSVPDCLSIMTYVSQYYNHFCSPGQAGVSPPRKGLAPCSPPSVAPTPVEPEDVAQGEELSSGSLSEQGTGQTPSSTCAACQQHVHLVQRYLADGRLYHRHCFRCRRCSSTLLPGAYENGPEEGTFVCAEHCARLGPGTRSGTRPGPFSQPKQQHQQQLAEDAKDVPGGGPSSSAPAGAEADGPKASPEARPQIPTKPRVPGKLQELASPPAGRPTPAPRKASESTTPAPPTPRPRSSLQQENLVEQAGSSSLVNGRLHELPVPKPRGTPKPSEGTPAPRKDPPWITLVQAEPKKKPAPLPPSSSPGPPSQDSRQVENGGTEEVAQPSPTASLESKPYNPFEEEEEDKEEEAPAAPSLATSPALGHPESTPKSLHPWYGITPTSSPKTKKRPAPRAPSASPLALHASRLSHSEPPSATPSPALSVESLSSESASQTAGAELLEPPAVPKSSSEPAVHAPGTPGNPVSLSTNSSLASSGELVEPRVEQMPQASPGLAPRTRGSSGPQPAKPCSGATPTPLLLVGDRSPVPSPGSSSPQLQVKSSCKENPFNRKPSPAASPATKKATKGSKPVRPPAPGHGFPLIKRKVQADQYIPEEDIHGEMDTIERRLDALEHRGVLLEEKLRGGLNEGREDDMLVDWFKLIHEKHLLVRRESELIYVFKQQNLEQRQADVEYELRCLLNKPEKDWTEEDRAREKVLMQELVTLIEQRNAIINCLDEDRQREEEEDKMLEAMIKKKEFQREAEPEGKKKGKFKTMKMLKLLGNKRDAKSKSPRDKS
Protein: Protein hunchback (P05084)
Organism: Drosophila melanogaster (Fruit fly)
Function: Gap class segmentation protein that controls development of head structures.
Subcellular location: Nucleus.
Interaction partners:
- Zygotic gap protein knirps
- Homeotic protein bicoid
- Segmentation protein even-skipped
- Protein tailless
- Huckebein
- POU domain protein 2, isoform B
- Segmentation protein fushi tarazu
- Transcription factor Zelda
- Kekkon 2
- Protein nanos
Sequence:
MQNWETTATTNYEQHNAWYNSMFAANIKQEPGHHLDGNSVASSPRQSPIPSTNHLEQFLKQQQQQLQQQPMDTLCAMTPSPSQNDQNSLQHYDANLQQQLLQQQQYQQHFQAAQQQHHHHHHLMGGFNPLTPPGLPNPMQHFYGGNLRPSPQPTPTSASTIAPVAVATGSSEKLQALTPPMDVTPPKSPAKSSQSNIEPEKEHDQMSNSSEDMKYMAESEDDDTNIRMPIYNSHGKMKNYKCKTCGVVAITKVDFWAHTRTHMKPDKILQCPKCPFVTEFKHHLEYHIRKHKNQKPFQCDKCSYTCVNKSMLNSHRKSHSSVYQYRCADCDYATKYCHSFKLHLRKYGHKPGMVLDEDGTPNPSLVIDVYGTRRGPKSKNGGPIASGGSGSGSRKSNVAAVAPQQQQSQPAQPVATSQLSAALQGFPLVQGNSAPPAASPVLPLPASPAKSVASVEQTPSLPSPANLLPPLASLLQQNRNMAFFPYWNLNLQMLAAQQQAAVLAQLSPRMREQLQQQNQQQSDNEEEEQDDEYERKSVDSAMDLSQGTPVKEDEQQQQPQQPLAMNLKVEEEATPLMSSSNASRRKGRVLKLDTLLQLRSEAMTSPEQLKVPSTPMPTASSPIAGRKPMPEEHCSGTSSADESMETAHVPQANTSASSTASSSGNSSNASSNSNGNSSSNSSSNGTTSAVAAPPSGTPAAAGAIYECKYCDIFFKDAVLYTIHMGYHSCDDVFKCNMCGEKCDGPVGLFVHMARNAHS
Protein: WASP-related protein (Q7KWP7)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Actin-related protein 2
- Actin-related protein 3
- Actin-related protein 2/3 complex subunit 1
- Actin-related protein 2/3 complex subunit 3
- Actin-related protein 2/3 complex subunit 5
- Actin-related protein 2/3 complex subunit 2
- Actin-related protein 2/3 complex subunit 4
- SH3 domain-containing protein
- Rho GTPase-activating protein gacF
- Serine/threonine-protein kinase pakF
Sequence:
MTEIDSHNPKTKKKHGRFFQKVLDKTRHRNEEKGMEISGPTDFKHESHIGWDKENGFEIKNIPPEWRQLFQAAGIKKKDLKNPETVQFIYSIIGENINNQKAGMAGGTTTAPYQQTNIPQQQQQQQQQQPIRSRAPPPPPPTSTTQKMGAQRVPPPKPGSEIRPLPKHQQINKPLPQQPYKQMAQQQPPQQQQQQQAYTTRGKLPTTIGGKPIPIHQNFMKPDDEPLQPTQPQQPQQQQIYNSNEPLIQQEFKSQYKLDEPLQPTQKRPSPQQMEQVMQSTSNGVQQYVYQQQNQKPQEYTFQGETPQQYVYQSSQQPQNLEGYNQFYQQKPLQPQQPQQVTPQRKQPTPPPRQRRDLSQQPSQTKLQSPPPPLPTSKRPGLPPTPPTQQRIPVVQPPIIQRTTQQPQVIIDKVGGDVMPPPPPPMPDQLAHIPVAPVDPKSPLPPAPSIQSPIEKPTPISLNNSSMVPPPPPPPSAPISLNNSSMVPPPPPAISKPTSAPPTSMPPLDSGRSNLMDSIRGFGGASHLKKVDPSEPLPDLKELQLGESGNRSLVDTLAAAMAKRRGNLGENEEDDEDDSDWEN
Protein: Nucleoporin NUP35 (35 kDa nucleoporin) (Mitotic phosphoprotein 44) (MP-44) (Nuclear pore complex protein Nup53) (Nucleoporin NUP53) (Q8NFH5)
Organism: Homo sapiens (Human)
Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. May play a role in the association of MAD1 with the NPC.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000269|PubMed:12196509}. Nucleus membrane {ECO:0000269|PubMed:15703211}; Peripheral membrane protein {ECO:0000269|PubMed:15703211}. Note=Tightly associated with the nuclear membrane and lamina. {ECO:0000269|PubMed:15703211}.
Interaction partners:
- Nuclear pore complex protein Nup93
- Nucleoporin NDC1
- Nucleoporin NUP188
- Nuclear pore complex protein Nup155
- Nuclear pore complex protein Nup205
- E3 SUMO-protein ligase RanBP2
- Nuclear pore complex protein Nup98-Nup96
- Nuclear pore complex protein Nup88
- Nuclear pore complex protein Nup153
- Nuclear pore glycoprotein p62
Sequence:
MAAFAVEPQGPALGSEPMMLGSPTSPKPGVNAQFLPGFLMGDLPAPVTPQPRSISGPSVGVMEMRSPLLAGGSPPQPVVPAHKDKSGAPPVRSIYDDISSPGLGSTPLTSRRQPNISVMQSPLVGVTSTPGTGQSMFSPASIGQPRKTTLSPAQLDPFYTQGDSLTSEDHLDDSWVTVFGFPQASASYILLQFAQYGNILKHVMSNTGNWMHIRYQSKLQARKALSKDGRIFGESIMIGVKPCIDKSVMESSDRCALSSPSLAFTPPIKTLGTPTQPGSTPRISTMRPLATAYKASTSDYQVISDRQTPKKDESLVSKAMEYMFGW