wanglab/gogpt-training-data huggingface dataset:
Protein: Kinesin-like protein KIF27 (Q7M6Z4)
Organism: Mus musculus (Mouse)
Function: Plays an essential role in motile ciliogenesis.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305|PubMed:19305393}. Cell projection, cilium {ECO:0000269|PubMed:19305393}. Note=Localizes to centrioles and basal bodies.
Interaction partners:
- Serine/threonine-protein kinase 36
- Protein smoothened
Sequence:
MEEIPIKVAVRIRPLLCKEVLHNHQVCVRDIPNTQQIIIGRDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFAYGQTGSGKTYTIGGGHVASVVEGQKGIIPRAIQEIFQSISENPSIDFKIKVSYIEVYKEDLRDLLELETSMKDLHIREDEKGNTVIVGAKECQVESVEDVMSLLQVGNAARHTGTTQMNEHSSRSHAIFTISVCQVEKNAEAAENGEWYSHRHIVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRRKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPSSSDFDESLNSLKYANRARNIRNKPALNISPQADRMDEMEFEIKLLREALQSHQASISQASQASSENVPDQNRIHSLEEQVAQLQEECLGYQDCIEQAFAFLVDLKDAVKLNQKQQHKLQEWFSRTQEVRKAVLTPLPGNQGIGNLEEGPQHLTVLQLKRELKKYQCALAADQVVFTQKDLELEELRTQVQLMMQESKGHAVSLKEAQKVNRLQNEKIIEQQLLVDQLSAELAKRSLSVPTSAKESCGDGPDARASEKRPHTAPFESHWGHYVYIPSRQDFKKVCSSTPVYSLDQVFAGFRTRSQMLMGHLEDQDEVLHCQFSDNSDDEDSEGQEKPRVRSRSHSWAKKPGSVCSLVELSDTQAESQRSYLGNGDLKMESLQESQEINLQKLRTSELILNKAKQKMRELTINIRMKEDLIKELIKTGNNAKSVSRQYSLKVTKLEHEAEQAKVELTETRKQLQELESKDLSDVALKVKLQKEFRKKMDAAKMRVQVLQKKQQDSKKLASLSIQNEKRASELEHNVDHLKYQKVQLQRRLREEGEKKKQLDAEIKRDQQKIKELQLKAGQGEGLNPKAEDQDGFNLNRRKSPFRSGDQFQKLDEQRKWLDEEVEKVLSQRQELEMLEEDLKKREAIVSKKEALLQEKSLLENKKLRSSQALSTDGLKISARLNLLDQELSEKSLQLESSPTEEKMKISEQVQALQRERDQLQRQRNSVDERLKHGRVLSPKEEHLLFQLEEGIEALEAAIEFKNESIQSRQNSLKASFQNLSQSEANVLEKLVCLNITEIRAILFKYFNKVINLRETERKQQLQNKEMKMKVLERDNVVHELESALEHLRLQCDRRLTLQQKEHEQKMQLLLQHFKDQDGDSIIETLKNYEDKIQQLEKDLYFYKKTSRDLKKRLKDPAQGAAQWQRTLTEHHDAGDGVLNPEETTVLSEELKWASRTENTKLNGSEREVDNSSSSLKTQPLTQQIPEDGPDSLPARSSIAPSSGQLQSIADKTEARPFTHSQSPVPHQFQPVRSIGPLQGVKPVKLCRRELRQISAMELSLRRCSLGAGGRSMTADSLEDPEEN
Protein: DNA polymerase subunit gamma-1, mitochondrial (EC 2.7.7.7) (3'-5' exodeoxyribonuclease) (EC 3.1.11.-) (DNA polymerase gamma subunit 1) (Mitochondrial DNA polymerase catalytic subunit) (Protein tamas) (Q27607)
Organism: Drosophila melanogaster (Fruit fly)
Function: As the catalytic component of the DNA polymerase gamma complex is involved in the replication of mitochondrial DNA (mtDNA). Has both 5'-3' DNA polymerase and a highly mispair-specific 3'-5' exonuclease activity. At the end of mtDNA replication DNA ends are ligated to produce a closed circular mtDNA molecule, its exonuclease activity is required for formation of these ligatable ends by preventing DNA synthesis from continuing past the 5'-end of downstream DNA into duplex DNA regions. Does not possess DNA primase activity, does not catalyze strand displacement synthesis and does not contain a 5'-3' exonuclease activity to catalyze nick translation. Important for promoting the elimination of paternal mitochondrial DNA during spermatogenesis, however its exact role in this function has not yet been identified and appears to be independent of its 3'-5'-exonuclease activity and only partially dependent on its DNA polymerase activity.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:28318978, ECO:0000269|PubMed:3095323}. Note=In sperm, detected in puncta that associate with mitochondrial nucleoids at developmental stages when the nucleoids are being eliminated. {ECO:0000269|PubMed:28318978}.
Interaction partners:
- DNA polymerase subunit gamma-2, mitochondrial
- Single-stranded DNA-binding protein, mitochondrial
- Mitochondrial DNA helicase
- DNA primase small subunit
- DNA polymerase delta catalytic subunit
- Mitochondrial transcription factor A, isoform B
- DNA polymerase alpha catalytic subunit
- Glycine--tRNA ligase
- DNA-directed RNA polymerase
- DNA primase large subunit
Sequence:
MQFHLIRKYASKVSREHYASSSVKIFRRVKPPQKVNKPKKPENVENGPTEYAENLVKVQMISRNLHAQLFPQAPRSISEQQVASAKVYKDELRRHGVDIESSAPVSDVQLKLPALRGANIEEHFHNIAKEQVQPYEELLLPLVQCEQLPKRPKRWAFHTGWTAYDPEDGTATPVDHPLEKGLVFDVEVCVSEGQAPVLATAVSTKRWYSWVSSKLTKHRLSVEKLEPLDVDTDSERPHYTTDELIPLGTTGPGLVVGHNVSYDRARLKEQYLTEDTGTRFVDTMSLHMCVSGVTSYQRAMLKSKKEPAAEDLGWLEQSSLNSLVEVHRLYCGGDTLSKEPRNIFVEGTLEQVRQSFQSLTNYCASDVEATHRILRVLYPLYAERFPHPASLAGMLEMGSAYLPVNSNWERYIREAQLTYEDLSIEAKYHLGRRAEEACSLLLDDQYRQNLWLWDEDWSVQELKLKQPPKRKPLPTVELKDSGNTPEERRLQAKFQHLYDQQALLPARRPLLPGYPLWYRKLCRKPPAKRADEILEDDEEPWSPGASEISTGMQIAPKLLSLCWEGYPLHYEREQGWGFLVPFRSDSEGVDRLPMEQLLAHCPVPEFARLSASKAESDMAFDMLPGQVEQHLGKREHYKKLSQKQQRLETQYQGSGVWCNKVLDDCCFFLKLPHKNGPSFRVGNPLSKDFLNKFAENVLSSGDPSCQAAARVIDIARMMSYWRNNRDRIMGQMVVWLDSQQLPNEFTGEKCQPIAYGAICPQVVACGTLTRRAMEPTWMTASNSRPDRLGSELRSMVQAPPGYRLVGADVDSQELWIASVLGDAYACGEHGATPLGWMTLSGSKSNGSDMHSITAKAVGISRDHAKVINYARIYGAGQLFAETLLRQFNPTFSASEAKAKAMKMFSITKGKRVYRLREEFHDELEDRAYSSYEASRLAIQRNRTLAEVFHRPNWQGGTESAMFNRLEEIATGSQPRTPFLGGRLSRALEADTGPEQEQRFLPTRINWVVQSGAVDFLHLMLVSMRWLMGSHVRFCLSFHDELRYLVKEELSPKAALAMHITNLMTRSFCVSRIGLQDLPMSVAFFSSVEVDTVLRKECTMDCKTPSNPHGLRIGYGIQPGQSLSVAEAIEKAGGNDVSQWDWIKKS
Protein: Tryptophan 2,3-dioxygenase (TDO) (EC 1.13.11.11) (Protein vermilion) (Tryptamin 2,3-dioxygenase) (Tryptophan oxygenase) (TO) (TRPO) (Tryptophan pyrrolase) (Tryptophanase) (P20351)
Organism: Drosophila melanogaster (Fruit fly)
Function: Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L-tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage of the indole moiety. Required during larval growth to control the level of potentially harmful free tryptophan in the hemolymph. In the adult the same reaction is the first step in the ommochrome biosynthetic pathway.
Interaction partners:
- Kynurenine formamidase
- Kynurenine 3-monooxygenase
- Tryptophan 5-hydroxylase 2
- Aromatic-L-amino-acid decarboxylase
- Nicotinate phosphoribosyltransferase
- Glutamine-dependent NAD
- FI04487p
- Tyrosine aminotransferase
Sequence:
MSCPYAGNGNDHDDSAVPLTTEVGKIYGEYLMLDKLLDAQCMLSEEDKRPVHDEHLFIITHQAYELWFKQIIFEFDSIRDMLDAEVIDETKTLEIVKRLNRVVLILKLLVDQVPILETMTPLDFMDFRKYLAPASGFQSLQFRLIENKLGVLTEQRVRYNQKYSDVFSDEEARNSIRNSEKDPSLLELVQRWLERTPGLEESGFNFWAKFQESVDRFLEAQVQSAMEEPVEKAKNYRLMDIEKRREVYRSIFDPAVHDALVRRGDRRFSHRALQGAIMITFYRDEPRFSQPHQLLTLLMDIDSLITKWRYNHVIMVQRMIGSQQLGTGGSSGYQYLRSTLSDRYKVFLDLFNLSTFLIPREAIPPLDETIRKKLINKSV
Protein: Nitric oxide synthase, inducible (EC 1.14.13.39) (Hepatocyte NOS) (HEP-NOS) (Inducible NO synthase) (Inducible NOS) (iNOS) (NOS type II) (Peptidyl-cysteine S-nitrosylase NOS2) (P35228)
Organism: Homo sapiens (Human)
Function: Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such PTGS2/COX2 (By similarity). As component of the iNOS-S100A8/9 transnitrosylase complex involved in the selective inflammatory stimulus-dependent S-nitrosylation of GAPDH on 'Cys-247' implicated in regulation of the GAIT complex activity and probably multiple targets including ANXA5, EZR, MSN and VIM. Involved in inflammation, enhances the synthesis of pro-inflammatory mediators such as IL6 and IL8.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:21199876}. Note=Localizes as discrete foci scattered throughout the cytosol and in the presence of SPSB1 and SPSB4, exhibits a more diffuse cytosolic localization. {ECO:0000269|PubMed:21199876}.
Interaction partners:
- Calmodulin-1
- Calmodulin-like protein 6
- Calmodulin-like protein 3
- Calmodulin-like protein 5
- Calmodulin-like protein 4
- Arginase-1
- Calmodulin-1
- RAC-alpha serine/threonine-protein kinase
- Argininosuccinate synthase
- Arginase-2, mitochondrial
Sequence:
MACPWKFLFKTKFHQYAMNGEKDINNNVEKAPCATSSPVTQDDLQYHNLSKQQNESPQPLVETGKKSPESLVKLDATPLSSPRHVRIKNWGSGMTFQDTLHHKAKGILTCRSKSCLGSIMTPKSLTRGPRDKPTPPDELLPQAIEFVNQYYGSFKEAKIEEHLARVEAVTKEIETTGTYQLTGDELIFATKQAWRNAPRCIGRIQWSNLQVFDARSCSTAREMFEHICRHVRYSTNNGNIRSAITVFPQRSDGKHDFRVWNAQLIRYAGYQMPDGSIRGDPANVEFTQLCIDLGWKPKYGRFDVVPLVLQANGRDPELFEIPPDLVLEVAMEHPKYEWFRELELKWYALPAVANMLLEVGGLEFPGCPFNGWYMGTEIGVRDFCDVQRYNILEEVGRRMGLETHKLASLWKDQAVVEINIAVLHSFQKQNVTIMDHHSAAESFMKYMQNEYRSRGGCPADWIWLVPPMSGSITPVFHQEMLNYVLSPFYYYQVEAWKTHVWQDEKRRPKRREIPLKVLVKAVLFACMLMRKTMASRVRVTILFATETGKSEALAWDLGALFSCAFNPKVVCMDKYRLSCLEEERLLLVVTSTFGNGDCPGNGEKLKKSLFMLKELNNKFRYAVFGLGSSMYPRFCAFAHDIDQKLSHLGASQLTPMGEGDELSGQEDAFRSWAVQTFKAACETFDVRGKQHIQIPKLYTSNVTWDPHHYRLVQDSQPLDLSKALSSMHAKNVFTMRLKSRQNLQSPTSSRATILVELSCEDGQGLNYLPGEHLGVCPGNQPALVQGILERVVDGPTPHQTVRLEALDESGSYWVSDKRLPPCSLSQALTYFLDITTPPTQLLLQKLAQVATEEPERQRLEALCQPSEYSKWKFTNSPTFLEVLEEFPSLRVSAGFLLSQLPILKPRFYSISSSRDHTPTEIHLTVAVVTYHTRDGQGPLHHGVCSTWLNSLKPQDPVPCFVRNASGFHLPEDPSHPCILIGPGTGIAPFRSFWQQRLHDSQHKGVRGGRMTLVFGCRRPDEDHIYQEEMLEMAQKGVLHAVHTAYSRLPGKPKVYVQDILRQQLASEVLRVLHKEPGHLYVCGDVRMARDVAHTLKQLVAAKLKLNEEQVEDYFFQLKSQKRYHEDIFGAVFPYEAKKDRVAVQPSSLEMSAL
Protein: At2g33360 (Cadherin EGF LAG seven-pass G-type receptor, putative (DUF3527)) (O22787)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MGSVSPDAQKDDLELEDSLNIDENLSGGNGLLKSGNLLSQKRQQCSLVSNSGKWLQIVKNGPKGSFSRATSFFDNKIPRQLVSVDEKYLRRCLDLINISAFKSASCSLSLNLVGSKMSLSSRRFDLPVIPKENVARLVFDLPLVDDSGSPVISRAIIGCKRVTYMLDKPTLHSLEALDGDGNNIGTRRDHNGESELVSYDVVRKIEEKNTPDSQFLSYHSGNMPRKAVSLSSTNSLSSSSSEQSSSSWSPSSSVSQGTLQFTMKDNKTPHFVFSLDDQKEIYVASLSTTSVGSGFDRSSLDYSYLIHLKKGRGSEPQHLVGKLKVSTLFSVSSTNEKTVERQFVLFSSGGNPQLPCHKDIRKNRGLPKKVVDALKSTKRTSRQRSISRFSRTSSIPDFCSWEPFQEHDSDLEPISLLDNDLPPNLETSAVVVREQFPVEEEEEEEVEKVGGWGMKFLKKIPLARTKDASKCSKHSTSIDVVIPLGIHGGPRNRNGGPSSLIQRWKSGGCCDCSGWDLGCPLTVLKGQARKDQSEGQCNLFELFTEGLMQGSPGLRIMNVRDGLYFVQSQAKISVLQSFSIALAYIHSQSQRLRPWSSKKCTEA
Protein: Conserved hypothetical proline rich protein (O53538)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Chaperone protein HtpG
- Protein GrpE
- Chaperone protein DnaJ 2
- Chaperone protein DnaJ 1
- Chaperonin GroEL 1
- Chaperonin GroEL 2
- Chaperone protein ClpB
- Uncharacterized protein Rv2667
- ATP-dependent Clp protease ATP-binding subunit ClpC1
- Co-chaperonin GroES
Sequence:
MATGARPALGLSIGVTNLAAVAADHSITRKPVLTLYRQRPPEVGVPSENPRLDEPGLVITDFVDRVGDSVGIVAADGSVYRSEALVADALLALAYTATGGRALPGSVTVTYPAHWGPAAVAALDSALRRASEWSHGTSSTAQPLSLLPDAAAALYAIRADPGIPARGIVAVCDFGGSGTGITLVDAADEYRPVAATVRHQAFSGDLIDQSLLSYVMSELPGTGAFDPAGTSAIGSLTKLRIECRKAKERLSSSTVTTLTDALGGDIRLTRNELEDTIRDSLDSVGRALEQTLARSGIRTAELVAIVSVGGGANIPAVTTTLSGRFCVPVVRTPRPQLTAAFGGALWAARRPGDTSATVLTAVTSATATAPADAPASVLQPALAWSEADEDSHIGPAPGYTAARPSLSFDHDAHAEPEPKSPPIPWYRLPAVIITGTTVAVLLVGAAVAIGLSTGDQPTAPGTPQRPGVTTTAAPPPSPAPASDGPTTEPAPPVQAPATGGPAPPLQQPLPPPPTTTNTQPAVTTDVITPAPTTPASAPPATTQPPATTQPPATTSPSPPPIPPIPPIPEIPQLPPGIPQVPGIGQFSAISGS
Protein: Axin-1 (Axis inhibition protein 1) (xAxin) (Q9YGY0)
Organism: Xenopus laevis (African clawed frog)
Function: Component of the beta-catenin destruction complex required for regulating ctnnb1 levels through phosphorylation and ubiquitination, and modulating Wnt-signaling. Controls dorsoventral patterning via two opposing effects; down-regulates ctnnb1 to inhibit the Wnt signaling pathway and ventralize embryos, but also dorsalizes embryos by activating a Wnt-independent JNK signaling pathway.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O15169}. Nucleus {ECO:0000250|UniProtKB:O15169}. Membrane {ECO:0000250|UniProtKB:O35625}. Cell membrane {ECO:0000250|UniProtKB:O35625}.
Interaction partners:
Sequence:
MSVKGKGFPLDLGGSFTEDAPRPPVPGEEGELITTDQRPFSHTYYSLKNDGIKNETSTATPRRPDLDLGYEPEGSASPTPPYLKWAESLHSLLDDQDGIHLFRTFLQQENCADLLDFWFACSGFRKLEPNDSKVEKRLKLAKAIYKKYVLDSNGIVSRQIKPATKSFIKDCVLRQQIDPAMFDQAQMEIQSMMEDNTYPVFLKSDIYLEYTTIGGESPKNYSDQSSGSGTGKGPSGYLPTLNEDEEWRCDQGGEHERERECIPSSLFSQKLALDSSSHCAGSNRRLSDGREFRPGTWREPVNPYYVNTGYAGAPVTSANDSEQQSMSSDADTMSLTDSSVDGIPPYRLRKHYRREMQESANANGRGPLPHIPRTYHMPKDIHVDPEKFAAELISRLEGVLRDREAEQKLEERLKRVRAEEEGDDGDVSSGPSVISHKLPSGPPMHHFNSRYSETGCVGMQIRDAHEENPESILDEHVQRVMKTPGCQSPGTGRHSPKSRSPDGHLSKTLPGSLGTMQTGHGKHSSKSTAKVDSGNLHHHKHVYHHVHHHGGVKPKEQIDGESTQRVQTNFPWNVESHNYATKSRNYAESMGMAPNPMDSLAYSGKVSMLSKRNAKKADLGKSESASHEMPVVPEDSERHQKILQWIMEGEKEIIRHKKSNHSSSSAKKQPPTELARPLSIERPGAVHPWVSAQLRNVVQPSHPFIQDPTMPPNPAPNPLTQLVSKPGARLEEEEKKAAKMPQKQRLKPQKKNVSAPSQPCDNIVVAYYFCGEPIPYRTMVKGRVVTLGQFKELLTKKGNYRYYFKKVSDEFDCGVVFEEVREDDMILPIYEEKIIGQVEKID
Protein: Eukaryotic translation initiation factor 4B (eIF-4B) (P34167)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in translation initiation. May be the homolog of mammalian eIF4B and be part of an RNA helicase. STM1/TIF3 is a non-essential gene.
Interaction partners:
- ATP-dependent RNA helicase eIF4A
- Eukaryotic translation initiation factor 4E
- Eukaryotic translation initiation factor 5
- Eukaryotic initiation factor 4F subunit p150
- Polyadenylate-binding protein, cytoplasmic and nuclear
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 5B
- Eukaryotic translation initiation factor 2 subunit gamma
Sequence:
MAPPKKTVKKMDLTSFLNDDTFGSSWAEEDVDLNKITIPIETANANTIPLSELAHAKNNSNNTRSGGFGGSFGGRSRLDPALGGGSSDRREEYPVPDAPPYRAVINNIPWDITPEGVQAWVEDGLVKPEAVEEVVLPKNLRDPTRLKGNAFVTLKERADLVAVLKFNGTKLNERTVYVSVAAPRRGGGADVDWSSARGSNFQGDGREDAPDLDWGAARGSNFRGPRREREEVDIDWTAARGSNFQGSSRPPRREREEVDIDWSAARGSNFQGSSRPPRREREEPDIDWSAARGSNFQSSSRPPRREREEPDIDWSAARGSNFQSSSRPPRREREKEEPALDWGAARGAQFGKPQQTKNTYKDRSLTNKKTTDEQPKIQKSVYDVLRTEDDDEDEEAEKQNGDAKENKVDAAVEKLQDKTAQLTVEDGDNWEVVGKK
Protein: SWR1 complex subunit 2 (F4IP06)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant H2A.F/Z leading to transcriptional regulation of selected genes (e.g. FLC) by chromatin remodeling.
Interaction partners:
- RuvB-like protein 1
- SWR1-complex protein 4
- RuvB-like helicase
- Protein PHOTOPERIOD-INDEPENDENT EARLY FLOWERING 1
- SWR1 complex subunit 6
- Actin-related protein 4
- RuvB-like helicase
- Transcription initiation factor TFIID subunit 14b
- Actin-related protein 6
- Probable histone H2A variant 2
Sequence:
MEIDEEEPMVFLDRTTRATRGKRMTKLLDDEVEEDEQFWNQEALKEEEHDDEYEAEREVADEFDSDFNDDEPEPDAVAVNEKELRDLPKKRLIYPGKTASKKKKKKTKVVSQLEYIPGDEKPGEELGNKEQEEKEENEAQEDMEGEKVIRKSTRTSVVVRQAERDALRAAIQATTKPIQRKKVGEEKRMTQEEMLLEAAQTEIMNLRNLERVLAREEEVKKKAIVHKAVYKGPQIRYHSKDGCNYLEFCNGASFNSELSTKSVPYPEKAVCVITGLPAKYRDPKTGLPYATRDAFKAIRERFMDEHDGLRKKMEMGDLFDTLVAKGFATKQKRTKIPKSNKSFSLRSSARFLSSESEEESEEDSD
Protein: High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A (EC 3.1.4.35) (Q8QZV1)
Organism: Rattus norvegicus (Rat)
Function: Specifically hydrolyzes the second messenger cGMP, which is a key regulator of many important physiological processes. Highly specific: compared to other members of the cyclic nucleotide phosphodiesterase family, has the highest affinity and selectivity for cGMP. Specifically regulates natriuretic-peptide-dependent cGMP signaling in heart, acting as a regulator of cardiac hypertrophy in myocytes and muscle. Does not regulate nitric oxide-dependent cGMP in heart. Additional experiments are required to confirm whether its ability to hydrolyze natriuretic-peptide-dependent cGMP is specific to heart or is a general feature of the protein (By similarity). In brain, involved in cognitive function, such as learning and long-term memory.
Subcellular location: Cell projection, ruffle membrane {ECO:0000250|UniProtKB:O76083}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O76083}. Golgi apparatus {ECO:0000250|UniProtKB:O76083}. Endoplasmic reticulum {ECO:0000250|UniProtKB:O76083}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:O76083}.
Interaction partners:
- Adenine phosphoribosyltransferase
- Hypoxanthine-guanine phosphoribosyltransferase
- GMP synthase
- Inosine triphosphate pyrophosphatase
- Guanylate kinase
- Guanylate cyclase soluble subunit alpha-2
- Atrial natriuretic peptide receptor 1
- Atrial natriuretic peptide receptor 2
- Guanylate cyclase soluble subunit alpha-1
- Guanylate cyclase 2G
Sequence:
MGAGSSSYRPKAIYLDIDGRIQKVVFSKYCNSSDIMDLFCIATGLPRNTTISLLTTDDAMVSIDPTMPANSERTPYKVRPVAVKQVSEREELVQGVLAQVAEQFSRAFKINELKAEVANHLAMLEKRVELEGLKVVEIEKCKSDIKKMREELAARNNRTNCPCKYSFLDNKKLTPRRDVPTYPKYLLSPETIEALRKPTFDVWLWEPNEMLSCLEHMYHDLGLVRDFSINPITLRRWLLCVHDNYRSNPFHNFRHCFCVTQMMYSMVWLCGLQEKFSQMDILVLMTAAICHDLDHPGYNNTYQINARTELAVRYNDISPLENHHCAIAFQILARPECNIFASVPPEGFRQIRQGMITLILATDMARHAEIMDSFKEKMENFDYSNEEHLTLLKMILIKCCDISNEVRPMEVAEPWVDCLLEEYFMQSDREKSEGLPVAPFMDRDKVTKATAQIGFIKFVLIPMFETVTKLFPIVEETMLRPLWESREHYEELKQLDDAMKELQKKTENLTSGATENAPEKTRDAKDNEDRSPPN
Protein: Peroxisome proliferator-activated receptor alpha (Nuclear receptor subfamily 1 group C member 1) (Q9N135)
Organism: Sus scrofa (Pig)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU004334}.
Interaction partners:
Sequence:
MVDTESPICPLSPLEADDLESPLSEEFLQEMGTIQEISQSIGEDSSGSFSFTDYQYLGSGPGSDGSVITDTLSPASSPSSVTYPVAPAGADESPSVALNIECRICGDKASGYHYGVHACEGCKGFFRRTIRLKLVYDKCDRSCKIQKKNRNKCQYCRFHKCLSAGMSHNAIRFGRMPRSEKAKLKAEILTCEHDLEDAETADLKSLAKRIYEAIKKNFNMNKVKARVILAGKASNNPAFCIRDMETLCMAEKTLVAKLVANGTQNKEAEVRIFHCCQCTSDVSVTELTEFAKSIXGFASLDLNDQVTLLKYGVYDAIFAMLSSVMNKDGMLVAYGNGFITREFLKSLRKPFCDIMEPKFDFAMKFNALELDDSDLSLFVAAIICCGDRPGLLNVGHIERMQEGIVHVLKLHLQTNHPDDVFLFPKLLQKLADLRQLVTEHAQLVQVIKKTEADAALHPLLQEIYRDMY
Protein: Probable kinetochore protein ndc80 (Q5B3B1)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity.
Subcellular location: Nucleus {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Associated with kinetochores. {ECO:0000250}.
Interaction partners:
- Probable kinetochore protein spc25
- Probable kinetochore protein nuf2
- Probable kinetochore protein spc24
- Uncharacterized protein
- Dis1/XMAP215 protein AlpA
- CorA family metal ion transporter
- Mitotic spindle checkpoint protein
- Aurora kinase
- Calmodulin-binding protein Sha1, putative
- Separin
Sequence:
MSQDTGLFSIKRPRETLGSVQNFSSLPQPSSALKRTSSIGYQNPPFTSQHTRSMSLLNSVGRPQQPNFQRSSSGGFGADPGLSSVRRSVSSNVFHGTSAGRPSFAPGSMSSNPASQSLQRRSSVFSRPSTGGAMGHQSFFTQVPSAAGVPRDPRPLRDRSFQARIAQELLEYLTHNNFELEMKHSLGQNTLRSPTQKDFNYIFQWLYHRIDPGYRFQKAMDAEVPPILKQLRYPYEKGITKSQIAAVGGQNWPTFLGMLHWLMELAQMMDRFAMGEYDEACAEMGVDVSGDRIIFRFLTGAYHDWLQGGEEEDDDAAAQRLIPHIELMAQEFEKGNEKYVQEMQVLDAENRALRDQIEELEKNAPDMAKLDKQFRILEDDKRKFEDYIQNVQGKIEKYESRIAFLEDEIRKTESELQAAEEERAGLQASVDQQGLTIQDIDRMNTERDRLQRSLDDAVSRLEETHARVMAKESEASAKLEDLEELVKTYNTLGYQNSLIPSTAVNANGQEYELGLNVNERSFSTSQIGGIPSRISPEADRLLAEPFTGYHPAHLLNLDLRGIVRSNLQALRKEINERRKRGIDADLERRNLLDNIKEAMDEKRSEVEALEHKRRTAEEEFERLKEVTTTQKLASDAQIEKMEKELAKMRATMSESVQLMEQREMNTNIEYEQLTLRANALREELHTNVESMLNDVIRFKVHIQKGLEDYENFVVDEVEQELGGDTQLDEDAPMSTEEL
Protein: RAD9 checkpoint clamp component A (F5H4F1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKCLVTGGNVKVLGKAVHSLSRIGDELYLEPLEDGLSLRTVNSSRSAYACFLFAPLFFQQYQAATPGQDLLRCKILMKTVEKCCISLNGRSSRLVVQLHCKFGVRKTHNLSFQDCESLQAVFDPASCPHMLRAPARVLGEAVLPFSPALAEVTLGIGRGRRVILRSYHEEEADSTAKAMVTEMCLGEEDFQQLQAQEGVAITFCLKEFRGLLSFAESANLNLSIHFDAPGRPAIFTIKDSLLDGHFV
Protein: Presenilins-associated rhomboid-like protein, mitochondrial (EC 3.4.21.105) (Mitochondrial intramembrane-cleaving protease Parl) (Rhomboid-7) (A1Z8R8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Mitochondrial intramembrane protease which plays a critical role in the regulation of mitochondrial function. Essential for mitochondrial development and fusion during spermatogenesis and the development of neurons and muscles. Essential for proteolytic processing of Pink1 and HtrA2 into their mature forms. May also be involved, but not required, for the proteolytic processing of Opa1.
Subcellular location: Mitochondrion inner membrane {ECO:0000305|PubMed:16713954}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Serine/threonine-protein kinase Pink1, mitochondrial
- ATP-dependent zinc metalloprotease YME1L
- Protein rhomboid
- E3 ubiquitin-protein ligase parkin
- Serine protease HTRA2, mitochondrial
- Transmembrane GTPase Marf
- Dynamin-like GTPase OPA1, mitochondrial
- Prohibitin
- LD34461p
- AFG3 like matrix AAA peptidase subunit 2, isoform A
Sequence:
MLMSRALCRSWLPQVARRCHANVNVPILRINSGHPAARSCRQIHSNRKQSSNLKPTTGEPAAAEQNTPVPVNNVIKAVAFTGAFTVGCFAGATILEYENTRSLILEKARQARFGWWQSRSLADRDYWTQIKQDIRRHWDSLTPGDKMFAPILLCNLVAFAMWRVPALKSTMITYFTSNPAAKVVCWPMFLSTFSHYSAMHLFANMYVMHSFANAAAVSLGKEQFLAVYLSAGVFSSLMSVLYKAATSQAGMSLGASGAIMTLLAYVCTQYPDTQLSILFLPALTFSAGAGIKVLMGIDFAGVVMGWKFFDHAAHLGGAMFGIFWATYGAQIWAKRIGLLNYYHDLRRTKQK
Protein: FAD dependent oxidoreductase domain-containing protein (Q2U0E2)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Interaction partners:
- Uncharacterized protein
- Serine hydroxymethyltransferase
- Serine hydroxymethyltransferase
- Glycine cleavage system P protein
- alanine--glyoxylate transaminase
- Aromatic amino acid beta-eliminating lyase/threonine aldolase domain-containing protein
- Aromatic amino acid beta-eliminating lyase/threonine aldolase domain-containing protein
- 5-aminolevulinate synthase
Sequence:
MTSSKLTPTSSILIVGAGTWGCSTALHLARRGYKNVTVLDPHPVPSPIAAGNDINKIMEHREVKASETDPWSIAFSTCTRAALKGWKNDPVFQPYFHETGAIVSGHTASLIKHIQEHEIDSSDAEFIKLNTAEDFRKTMPPGILTGNFPGWKGWLNKTGAGWIHAKKAMFSAYTEAKRLGVTFITGSPEGDVVSLIYENGDVVGARTADGTVHRADHTILSAGAGSDRLLDFKKQLRPTAWTLCHIRMTPDEAKKYRNLPVLFNVAKGFFMEPDEDNHELKICDEHPGYCNFVPDPKHGGEVRSIPFAKHQIPLEAEARARDFLRDTMPHLADRPLSFARICWDADTVDRAFLIDRHPEYRSLLLAVGGSGNGAMQMPTIGGFIADALEGNLQKELKHALRWRPEIAAQRDWKDTQNRFGGPNKVMDFQKVGENEWTKIGDKSRL
Protein: Adenylate kinase isoenzyme 6 homolog (AK6) (EC 2.7.4.3) (Dual activity adenylate kinase/ATPase) (AK/ATPase) (PfAKLP1) (Q8I236)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Broad-specificity nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. Has also ATPase activity.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03173, ECO:0000269|PubMed:22819813}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03173}.
Interaction partners:
- GTP:AMP phosphotransferase
- 40S ribosomal protein S11
- Ribonucleoside-diphosphate reductase
- Adenylosuccinate lyase
- nucleoside-diphosphate kinase
- Nucleoside diphosphate kinase
- Adenylate kinase 2
- Adenylate kinase 1
- Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase beta
- Pyruvate kinase
Sequence:
MKRKVPNIIITGVPGSGKSTLCEELKEIINKELLKRNDMEGFEMTHLNLSNIIKDERLYKEFDDELDASIYSEELLNEYLKKKYKLEKGGYIIDFHDINFVKDVDIIDKIFLLTIQTNFLYERLEKRNYTKEKIKNNIECEIFQVIKEDILDHFPNTNILQEIENNDLQQYDNNLSIIKNWVLSYI
Protein: Homocitrate dehydratase, mitochondrial (EC 4.2.1.-) (Aconitase 2) (P39533)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the reversible dehydration of (R)-homocitrate to cis-homoaconitate, a step in the alpha-aminoadipate pathway for lysine biosynthesis.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}.
Interaction partners:
- Homocitrate synthase, mitochondrial
- Homocitrate synthase, cytosolic isozyme
- Homoaconitase, mitochondrial
- Citrate synthase, peroxisomal
- Citrate synthase, mitochondrial
- Citrate synthase 3, mitochondrial
- Isocitrate dehydrogenase subunit 2, mitochondrial
- Aconitate hydratase, mitochondrial
- Homoisocitrate dehydrogenase, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
Sequence:
MLSSANRFYIKRHLATHANMFPSVSKNFQTKVPPYAKLLTNLDKIKQITNNAPLTLAEKILYSHLCDPEESITSSDLSTIRGNKYLKLNPDRVAMQDASAQMALLQFMTTGLNQTSVPASIHCDHLIVGKDGETKDLPSSIATNQEVFDFLESCAKRYGIQFWGPGSGIIHQIVLENFSAPGLMMLGTDSHTPNAGGLGAIAIGVGGADAVDALTGTPWELKAPKILGVKLTGKLNGWSTPKDVITKLAGLLTVRGGTGYIVEYFGEGVSTLSCTGMATICNMGAEIGATTSTFPYQEAHKRYLQATNRAEVAEAADVALNKFNFLRADKDAQYDKVIEIDLSAIEPHVNGPFTPDLSTPISQYAEKSLKENWPQKVSAGLIGSCTNSSYQDMSRVVDLVKQASKAGLKPRIPFFVTPGSEQIRATLERDGIIDIFQENGAKVLANACGPCIGQWNREDVSKTSKETNTIFTSFNRNFRARNDGNRNTMNFLTSPEIVTAMSYSGDAQFNPLTDSIKLPNGKDFKFQPPKGDELPKRGFEHGRDKFYPEMDPKPDSNVEIKVDPNSDRLQLLEPFKPWNGKELKTNVLLKVEGKCTTDHISAAGVWLKYKGHLENISYNTLIGAQNKETGEVNKAYDLDGTEYDIPGLMMKWKSDGRPWTVIAEHNYGEGSAREHAALSPRFLGGEILLVKSFARIHETNLKKQGVLPLTFANESDYDKISSGDVLETLNLVDMIAKDGNNGGEIDVKITKPNGESFTIKAKHTMSKDQIDFFKAGSAINYIGNIRRNE