wanglab/gogpt-training-data huggingface dataset:
Protein: Serine/threonine-protein kinase PAK 3 (EC 2.7.11.1) (Beta-PAK) (Oligophrenin-3) (p21-activated kinase 3) (PAK-3) (O75914)
Organism: Homo sapiens (Human)
Function: Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, or cell cycle regulation. Plays a role in dendrite spine morphogenesis as well as synapse formation and plasticity. Acts as downstream effector of the small GTPases CDC42 and RAC1. Activation by the binding of active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates MAPK4 and MAPK6 and activates the downstream target MAPKAPK5, a regulator of F-actin polymerization and cell migration. Additionally, phosphorylates TNNI3/troponin I to modulate calcium sensitivity and relaxation kinetics of thin myofilaments. May also be involved in early neuronal development. In hippocampal neurons, necessary for the formation of dendritic spines and excitatory synapses; this function is dependent on kinase activity and may be exerted by the regulation of actomyosin contractility through the phosphorylation of myosin II regulatory light chain (MLC) (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Rho guanine nucleotide exchange factor 7
- Cell division control protein 42 homolog
- Rho guanine nucleotide exchange factor 6
- Serine/threonine-protein kinase PAK 1
- SH2/SH3 adapter protein NCK1
- Serine/threonine-protein kinase PAK 2
- Ras-related C3 botulinum toxin substrate 2
- Cytoplasmic protein NCK2
- Ras-related C3 botulinum toxin substrate 3
- Ras-related C3 botulinum toxin substrate 1
Sequence:
MSDGLDNEEKPPAPPLRMNSNNRDSSALNHSSKPLPMAPEEKNKKARLRSIFPGGGDKTNKKKEKERPEISLPSDFEHTIHVGFDAVTGEFTPDLYGSQMCPGKLPEGIPEQWARLLQTSNITKLEQKKNPQAVLDVLKFYDSKETVNNQKYMSFTSGDKSAHGYIAAHPSSTKTASEPPLAPPVSEEEDEEEEEEEDENEPPPVIAPRPEHTKSIYTRSVVESIASPAVPNKEVTPPSAENANSSTLYRNTDRQRKKSKMTDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPERLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLKLAKPLSSLTPLIIAAKEAIKNSSR
Protein: DUF1618 domain-containing protein (Q388A2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVVIHSGLVTPVLEIMSLVKPLPFDVDVLLDEHPDMTVYHRPPLRSRGSGSKYICNHHPVELLSYEVYLCDTEDEPVVDFEVDNQIVVRYQLNPYCAASEFPFPRVFGNTIYRNQRPYLRPAYVEVAHGSGGCCFNGSGSSYGINVCVAPTDIFAGFPRSNNGDDAVIYSTVPHIRKLLQRPFSPFMECGPLIADDVFFHWDTLGLLSLTDTCDLGMFTIEGVCGVSSHIM
Protein: Bromodomain containing 8 (A0A8I6ATL0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MRKGQLTLSLKSALCPVLFGFEVASPCVDEQPHVHGLKTYTLMLLQRVNLCSVSGTPEVWPLWGLSTVISFRVVPGSNSGCRAFRTRVSVSRAIKPFAEPGRPPDWFSQKHCASQYSELLETTETPKRKRGEKGEVVETVEDVIVRKLTAERVEELKKVIKETQERYRRLKRDAELIQAGHMDSRLDELCSDIAMKKKLEEEEAEVKRKATDAAYQARQAVKTPPRRLPTVMVRSPIDSASPGGDYPLGDLTPTTMEEATSGVTPGTLPSTPVTSFPGIPDTLPPGSAPLEAPMTPVTDDSPQKKMLGQKATPPPSPLLSELLKKGSLLPTSPRLVNESEMPVPSGHLSSTGVLLEVGGVLPMIHGGDIQPATSAVAASPAASGAPTLSRLLEAGPTQFSTPLPSFTTVASEPPVKLVPPPVESVSQATIVMMPALPAPSSAPAVSTPESVAPVSQPEPCVPLEAVGDPQTVTVSMDSSEISMIINSIKEECFRSGVAEAPGGSKAPSIDGKEDLDLAEKMDIAVSYTGEELDFETVGDIIAIIEDKVDDHPEVLDVAAVEAALSFCEENDDPQSLPGPWEHPIQQERDKPVPLPAPEMTVKQERLDFEESETKGIHELVDIRDSGVEIKVEPTEPEPGMSGAEIVAGVGPVPSLEPPELRSQDLDEEPRSSAAGEMGEADGSSGKGEERPLPAVKTEASPESMLSPSHGSNPIEDPLEAETQHKFEMSDSLKEESGTIFGSQIKDAPGEEEEEDGVSEAASLEEPKEEDQGEGYLSEMDNEPPVSESDDGFSIHNATLQSHTLGDSIPSSPASSQFSVCSEDQEAIQAQKIWKKAIMLVWRAAANHRYANVFLQPVTDDIAPGYHSIVQRPMDLSTIKKNIENGLIRSTAEFQRDIMLMFQNAVMYNSSDHDVYHMAVEMQRDVLEQIQQFLATQLIMQTSESGISAKSLRGRDSTRKQDASEKDSVPMGSPAFLLSLFDGGTRGRRCAIEADMKMKK
Protein: Probable membrane transporter protein MamO (Q93DZ1)
Organism: Magnetospirillum gryphiswaldense (strain DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1)
Function: Plays 2 roles; promotes magnetite nucleation/formation and activates the MamE protease (By similarity). Despite its near conservation of a protease-like sequence, this is probably not a protease (By similarity). Required in conjunction with MamP for proteolysis of at least MamE, itself and MamP (By similarity). May transport a solute that controls MamE's protease activity. May place individual iron atoms into the magnetite lattice (By similarity). One of 7 genes (mamLQBIEMO) able to induce magnetosome membrane biogenesis; coexpression of mamLQRBIEMO in a deletion of the 17 gene mamAB operon restores magnetosome vesicle formation but not magnetite biosynthesis.
Subcellular location: Magnetosome membrane {ECO:0000269|PubMed:14766587}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Multi-heme protein MamP
- Actin-like protein MamK
- Magnetosome protein MamH
- Magnetosome protein MamQ
- Magnetosome protein MamM
- Magnetosome protein MamN
- Magnetosome protein MamB
- Magnetosome protein MamL
- Magnetosome protein MamS
- Magnetosome protein MamR
Sequence:
MIEIGETMGDQPTNKIVFCERSWKAPVSILAFLILVTFAWGAYLLDNYDEDDYFRGSDDMSVGQFLVRNVAMPDVQRLYYTVPPAVVGVGGGGVNAGPVASGAIVGANGYVITTLHSVANVPDITVQVATSAGIRRFPAQVVKTIPGHNLALLKLQTTEKFLHFRMANIQTVVPGQQVFAFGRNMAGAPLVRQGMVQSSDAPLAVGTTQITHLLRSDAVYSWEQTGGPLVNAQGDLVGINIAATGPTGKVEGFTVPAQVIVSHLQDVVRFKTGGAAGVAPPAAQTVAMGSSSWWSKAKAVVGGPTAVPGMGMNVVQGTVTTGIPSGMPFVDTDHVGGAKIGGYSIADILGLGMLALAAGVTGGMMTMGGGVLQVAGMMVFFGYGMYLIRPVVFLTNVVVYGAAALRNDKAQLVQWDKVKPLIPWGVAGVVIGYFIGNAIGDSVVGVLLGLFALIMAGKAVLEILQPNAGEDTAEAIAAAEAGDEMDELMALAEGTTRPKTSGIALPEGPTRSAVLGLPMGLFSGILGISGGVIEVPLQRYIGRISLQNAIANSSVLVFWASVAGSVVAFIHGGSTGLIHWEAPVTLALVMIPGAYVGGILGARLMRVLPVRVLKGIYAATMAAIAIKMLTTV
Protein: Histone H2A.1 (Q59SU5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
Interaction partners:
- Histone H2B.1
- Histone H4
- Histone H2B.2
- Histone H3.1/H3.2
- Histone H2A.Z
- Histone H3-like centromeric protein CSE4
- Histone H3.3
- FACT complex subunit SPT16
- Histone-lysine N-methyltransferase, H3 lysine-36 specific
- DNA-directed RNA polymerase subunit beta
Sequence:
MSGGKGKAGTSEKASTSRSAKAGLTFPVGRVHRLLRKGNYAQRIGSGAPVYLTSVLEYLAAEILELAGNAARDNKKSRIIPRHLQLAIRNDEELNKLLGDVTIAQGGVLPNIHQNLLPKKSGKGGVKASQEL
Protein: UPF0743 protein C215.06c (O94311)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Ribosome production factor 2 homolog
- H/ACA ribonucleoprotein complex subunit nhp2
- Brix domain-containing protein C1B9.03c
- Protein pxr1
- Ribosomal RNA-processing protein 14-C
- Ribosomal RNA-processing protein 1 homolog
- ATP-dependent RNA helicase has1
- Uncharacterized RNA-binding protein C1827.05c
- Ribosome biogenesis regulatory protein homolog
- Ribosome assembly factor mrt4
Sequence:
MVSFCCEVCQDIIKKPKLDQHRSRCHGAYFTCIDCNTTFERTDYRNHTSCMTEAQRYQKGLYRPTKKELKKAKMNGNAVNSKELSPNTDNQNTPAGPTKHSLDENEKDKENKKSKKETVSSPAEQLLALTQNQEISLYKLLKKYNKQASKEDSLDSKEVLKHLAITADAKGNYLVKPITK
Protein: Histidine protein methyltransferase 1 (EC 2.1.1.85) (Mitotic exit network interactor 1) (P40481)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Protein-histidine N-methyltransferase that mediates methylation of RPL3 at 'His-243'. Methylates ribosome-associated RPL3, but not free RPL3, thereby regulating 60S subunit assembly. In addition to RPL3, mediates His methylation of other proteins.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Protein-lysine N-methyltransferase EFM2
- Protein-lysine N-methyltransferase EFM4
- Large ribosomal subunit protein uL3
- Ribosomal lysine N-methyltransferase 2
- Protein-lysine N-methyltransferase EFM6
- Protein-lysine N-methyltransferase EFM3
- Alpha N-terminal protein methyltransferase 1
- Ribosomal lysine N-methyltransferase 5
- Ribosomal lysine N-methyltransferase 3
- Protein arginine N-methyltransferase 2
Sequence:
MSFSFGFTSNDFDDDELVAQPETFVESSKENENTTAYINPLDSDFLSQAGVVQPNVEDLGTILESLKDVRLTFEEFQSPIYRKPLIKRELFDVKHQLMLETDAQSNNNSTELDILLGDTSEDLRKNIYEGGLKSWECSYDLVDLLSENVDRISNDIDAVVEIGCGTALPSEFLFRSALLRNDRSKGLKFVLTDYNASVLRLVTIPNLVITWAKTVLTKEQWYALQKDECEDIPINNEELLLTSKLLAAFYDDVQSRNISVTLISGSWGRKFSNLIHEVLSGSQKVLSLSSETIYQPDNLPVIAETILDIHNLPQTDVKTYVAAKDIYFGVGGSITEFEAYLDDKINSEHLPIHSERFKVNSGLKRSIICIETNKAIR
Protein: Contig An12c0160, genomic contig (EC 1.10.3.2) (A2QZQ7)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Interaction partners:
Sequence:
MLLEICWTALVHFFSFQSLFSSQQYPLPPNGGVEYPTSPTAAAGQADPSDMLEFPPLGAIDGFTCQYPGLKNKYIALPDGNQSLWLQPLEKDIQDEQYDIDTDYEIKAPTGVIRDVYVNVTKLASDKALKPDGVAFPEGKYINGSYPGPRIQACWGDTVRVHVTNKVDKNGTAIHMHGIRMLNTGYSDGVPGVTQCPIAVNDTFTYEFQAVQYGTTWYHSHYSLQYTDGMLGPLTIYGPASSAFAKWTYQVVEKHGPRIPMASILINDKGSFAGHYQDNRYKTDKLKPGKKYLLRLINAATDTAFIFSIDEHKMKVIGADLVPVEPYDMESIYIGIGQRYHVIVETKSEPEDTNRNYWIRTWPATGCHNFDCEPNERQGIFQYNPNDTEDPISTPYRPPYGGQCRDEDHDKLIPMFPWTVPKPTPDQLKRVTFPFDVLKQDNFTMPPEGWNGTDPTWSAWEVNGAPAWVNYQDLTINHLDDNHTWPANAALFELNSDPNSDEPTWAYMVIDGGHQDEEEKPPGESIIPAAHPMHLHGHDFALLKQSYDSFDDDVARDPDAMQGFIESLTYKNPARRDVVLLPKNGYVVIAFKLDNPGTWLLHCHIAWHASGGLALQILEDKDKVQELLKKDINPDQTARAQIDDGCAGWKKWWDKKENRWNPDARFQDDSGV
Protein: Pigment dispersing factor homolog pdf-2 (G5EGC3)
Organism: Caenorhabditis elegans
Function: Probable ligand of isoforms a and b of the calcitonin receptor-like protein, pdfr-1, a G-protein coupled receptor. May not signal through isoform c of pdfr-1. Involved in locomotion; may play a role in circadian rhythms of locomotor activity. Modulator of egg-laying.
Interaction partners:
- Pigment dispersing factor homolog pdf-1
- Calcitonin receptor-like protein 1
- Neuropeptide-Like Protein
Sequence:
MSSRISVSLLLLAVVATMFFTANVVDATPRSQGNMMRYGNSLPAYAPHVLYRFYNSRQFAPINKRNNAEVVNHILKNFGALDRLGDVGK
Protein: AT3g53630/F4P12_330 (Q8VXU5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSSFNGNSNIDNLLIQTLLGRLQIRPPNSHFLSQSLDDLLFKSDDSDGDDDGEGQTSLDREEARLEKELIRVIVSGRSDSLKPNSGQAVTVNEHHICVGFHEDEESDYRVWEWHGHIMLFDEENGYTPEYIYGNYFERLPVKLPNNRRVEKEKKKEMKEEEVENLGLRELIDGGDAAPGRILHRNNINIGSSRV
Protein: ABC-type oligopeptide transporter ABCB9 (EC 7.4.2.6) (ATP-binding cassette sub-family B member 9) (ATP-binding cassette transporter 9) (ABC transporter 9 protein) (hABCB9) (TAP-like protein) (TAPL) (Q9NP78)
Organism: Homo sapiens (Human)
Function: ATP-dependent low-affinity peptide transporter which translocates a broad spectrum of peptides from the cytosol to the lysosomal lumen for degradation. Displays a broad peptide length specificity from 6-mer up to at least 59-mer peptides with an optimum of 23-mers. Binds and transports smaller and larger peptides with the same affinity. Favors positively charged, aromatic or hydrophobic residues in the N- and C-terminal positions whereas negatively charged residues as well as asparagine and methionine are not favored.
Subcellular location: Lysosome membrane {ECO:0000269|PubMed:10748049, ECO:0000269|PubMed:15577206, ECO:0000269|PubMed:17897319, ECO:0000269|PubMed:17977821, ECO:0000269|PubMed:18175933, ECO:0000269|PubMed:18952056, ECO:0000269|PubMed:20377823, ECO:0000269|PubMed:21212514, ECO:0000269|PubMed:22641697, ECO:0000269|PubMed:30877195}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:10748049, ECO:0000269|PubMed:15577206, ECO:0000269|PubMed:17897319, ECO:0000269|PubMed:17977821, ECO:0000269|PubMed:18175933, ECO:0000269|PubMed:18952056, ECO:0000269|PubMed:20377823, ECO:0000269|PubMed:21212514}. Note=May be located in membrane rafts. Takes an intracellular route from the endoplasmic reticulum (ER), via Golgi and early endosomes to late endosomal and lysosomal compartments (PubMed:30877195). {ECO:0000269|PubMed:30877195}.
Interaction partners:
- Lysosome-associated membrane glycoprotein 2
- Lysosome-associated membrane glycoprotein 1
- Antigen peptide transporter 2
- Tapasin
- ABC-type antigen peptide transporter
Sequence:
MRLWKAVVVTLAFMSVDICVTTAIYVFSHLDRSLLEDIRHFNIFDSVLDLWAACLYRSCLLLGATIGVAKNSALGPRRLRASWLVITLVCLFVGIYAMVKLLLFSEVRRPIRDPWFWALFVWTYISLGASFLLWWLLSTVRPGTQALEPGAATEAEGFPGSGRPPPEQASGATLQKLLSYTKPDVAFLVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKVFEFIDRQPTMVHDGSLAPDHLEGRVDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQRQMLGLQPAADFTAGHNEPVANGSHKA
Protein: Carboxy-S-adenosyl-L-methionine synthase (Cx-SAM synthase) (EC 2.1.3.-) (O25150)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Function: Catalyzes the conversion of S-adenosyl-L-methionine (SAM) to carboxy-S-adenosyl-L-methionine (Cx-SAM).
Interaction partners:
- tRNA U34 carboxymethyltransferase
- Superoxide dismutase
Sequence:
MKDTLFNESLNKRFCFDEKVAHVFDDMLERSIPYYHEMLNLGAYFIAQNLKENIYPKSLPKPLIYDLGCSTGNFFIALNRQIQQEIELVGIDNSMPMLKKAQEKLKDFNNARFECMDFLEVEFKEASAFSLLFVLQFVRPMQREVLLKKIYNSLALNGVLLVGEKIMSEDRILDKQMIELYYLYKQNQGYSHNEIAFKREALENVLVPYSLKENVALLESVGFKHVEALFKWVNFTLLVARKT
Protein: Putative ribosome associated protein (G0RYD6)
Organism: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (Thermochaetoides thermophila)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Putative heat shock protein
- Uncharacterized protein
- Heat shock protein 70-like protein
- SGF29 C-terminal domain-containing protein
- Endoplasmic reticulum chaperone BiP
- Iron-sulfur cluster biogenesis chaperone
- Ribosome-associated molecular chaperone SSB1
Sequence:
MNATVVSLPLPTLPEGWAAEKDFKAIGKLTQEGSSMRTLEPVGPHFLAHARRVRHKRTFSEDDRIQAQAKAKKIEQDSDSDISEEEDPMLLARDAKDWKTQDHYKVLGLSKYRWRATEDQIKRAHRKKVLKHHPDKKAAAGRADDDNFFKCIQKAAEILLDPVKRRQFDSVDEEADIPPPTKKQLAKGNYYELWGKVFENEARFSKIQPVPGFGNENSTREEVEAFYNFWYNFDSWRSFEYLDEDVPDDNENRDQKRHMERKNANARKKKKAEDNARLRKLVEEAQAGDERIKRFRQEANAAKNKKRLEREAAERKAAEEARLKKEAEERARKEAEEKAKAEREAAKKAKEAAKNAVKKNKRVLRGSVKEANYFVEGEASAATIDAVLNDVDLVITKIDADEIAALAGKLNGLTVADEIKNVWKEEVSRLVGAGKLKEGDIKALVA
Protein: Uncharacterized protein C162.06c (O74422)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Vacuolar protein sorting-associated protein vts1
- Vacuolar protein-sorting-associated protein 46
- Vacuolar protein sorting-associated protein ist1
- ESCRT-III complex subunit did4
- Vacuolar protein sorting-associated protein 20
- Suppressor protein of bem1/bed5 double mutants
- Vacuolar protein sorting-associated protein 24
- Vacuolar-sorting protein snf7
- 3,4-dihydroxy-2-butanone 4-phosphate synthase
- Vacuolar protein-sorting-associated protein 25
Sequence:
MHRLFGRKPPTQPTASLTDAIDSLDKRSDSVEVKIAKLDAQLSVFQQKIANTRPGPGQTALKQRAMNVLRQKKIYESQLQQLQQQSFNMEQAAMTTESLKNTMATVQTMQETARQLKSQSKNVSIEKIEKLQDEIQDYMDAAGELNEVLGQNMTDINVDEEELDAELEALQQESSWLGDQSTAEKPSYLMPSNELPNFVDEEVAEPSTAQ
Protein: Homogentisate 1,2-dioxygenase (EC 1.13.11.5) (Homogentisate oxygenase) (Homogentisic acid oxidase) (Homogentisicase) (O09173)
Organism: Mus musculus (Mouse)
Function: Catalyzes the conversion of homogentisate to maleylacetoacetate.
Interaction partners:
- 4-hydroxyphenylpyruvate dioxygenase
- Maleylacetoacetate isomerase
- Fumarylacetoacetase
- Phenylalanine-4-hydroxylase
- 4-hydroxyphenylpyruvate dioxygenase-like protein
- Coagulation factor XIII B chain
- Alanine--glyoxylate aminotransferase 2, mitochondrial
- Tyrosine aminotransferase
- BLOC-3 complex member HPS4
- Oxaloacetate tautomerase FAHD1, mitochondrial
Sequence:
MAELKYISGFGNECASEDPRCPGSLPKGQNNPQVCPYNLYAEQLSGSAFTCPRNTNKRSWLYRILPSVSHKPFESIDQGHVTHNWDEVGPDPNQLRWKPFEIPKASEKKVDFVSGLYTLCGAGDIKSNNGLAVHIFLCNSSMENRCFYNSDGDFLIVPQKGKLLIYTEFGKMSLQPNEICVIQRGMRFSVDVFEETRGYILEVYGVHFELPDLGPIGANGLANPRDFLIPVAWYEDRRVPGGYTVINKFQGKLFACKQDVSPFNVVAWHGNYTPYKYNLENFMVINAVAFDHADPSIFTVLTAKSLRPGVAIADFVIFPPRWGVADKTFRPPYYHRNCMSEFMGLIKGHYEAKQGGFLPGGGSLHSAMTPHGPDADCFEKASKAKLEPERIADGTMAFMFESSLSLAVTKWGLKTCSCLDENYYKCWEPLRSHFTPNSRSPTEPK
Protein: 4-oxalomesaconate tautomerase (EC 5.3.2.8) (Gallate degradation protein D) (Q88JY0)
Organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
Function: Catalyzes the tautomerization of the 4-oxalomesaconic acid keto (OMAketo) generated by GalA dioxygenase to 4-oxalomesaconic acid enol (OMAenol). Mediates the second step in gallate degradation pathway.
Interaction partners:
- 4-oxalmesaconate hydratase
- 4-carboxy-4-hydroxy-2-oxoadipic acid aldolase
- Gallate dioxygenase
- 4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase
- HTH-type transcriptional regulator GalR
- Enoyl-CoA hydratase-isomerase
- enoyl-CoA hydratase
- Enoyl-CoA hydratase/isomerase family protein
- Enoyl-CoA hydratase/isomerase family protein
- Vanillate O-demethylase oxygenase subunit
Sequence:
MGQTRIPCLLMRGGTSKGAYFLHDDLPAPGPLRDRVLLAVMGSPDARQIDGIGGADSLTSKVAIIRASQRDDADVDYLFAQVVVDEARVDYGQNCGNILAGVGPFALERGLVAASGASTPVRIFMENTGQIAVAQVPTADGQVEYAGDTRIDGVPGRAAALVVTFADVAGASCGALLPTGNSRDCVEGVEVTCIDNGMPVVLLCAEDLGVTGYEPCETLEADSALKTRLEAIRLQLGPRMNLGDVSQRNVPKMCLLSAPRNGGTVNTRSFIPHRCHASIGVFGAVSVATACLIEGSVAQGLASTSGGDRQRLAVEHPSGEFTVEISLEHGVIKGCGLVRTARLLFDGVVCIGRDTWGGPEK
Protein: DNA replication licensing factor mcm2 (EC 3.6.4.12) (Cell division control protein 19) (Minichromosome maintenance protein 2) (P40377)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts as component of the mcm2-7 complex (mcm complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the mcm2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity (By similarity). Plays an important role in DNA replication.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- DNA replication licensing factor mcm5
- DNA replication licensing factor mcm7
- Cell division control protein 45 homolog
- DNA replication licensing factor mcm4
- Cell division control protein 18
- DNA replication complex GINS protein psf1
- DNA replication licensing factor mcm3
- DNA replication licensing factor mcm6
- Origin recognition complex subunit 1
- DNA replication complex GINS protein psf2
Sequence:
MDSFRKRGRRDSESLPFESENSSLGATPLSLPPSSPPPEFSDEAAEALVEEDIEDLDGEALDVEDEEGEDLFGEGMERDYQQNLELDRYDIEELDDDNDLEELDIGARRAVDARLRRRDIELDAAAGRTKPAAFLQDEDDDLDSNLGTGFTRHRHRIYDEYSPNVGALDESGELPLESIADVKADSIAEWVTLDPVRRTIAREFKNFLLEYTDENGTSVYGNRIRTLGEVNAESLMVNYAHLGESKPILAYFLANAPAPIFRIFDRVALEATLLHYPDYERIHSDIHVRITNLPTCFTLRDLRQSHLNCLVRVSGVVTRRTGLFPQLKYIRFTCTKCGATLGPFFQDSSVEVKISFCHNCSSRGPFVINSERTVYNNYQRITLQESPGTVPSGRLPRHREVILLADLVDVAKPGEEIDVTGIYRNNFDASLNTKNGFPVFATIIEANHISQLDGSGNTDDDFSLSRLTDDEEREIRALAKSPDIHNRIIASMAPSIYGHRSIKTAIAAALFGGVPKNINGKHKIRGDINVLLLGDPGTAKSQFLKYVEKTAHRAVFATGQGASAVGLTASVRKDPITNEWTLEGGALVLADKGVCLIDEFDKMNDQDRTSIHEAMEQQSISISKAGIVTTLQARCTIIAAANPIGGRYNTTIPFNQNVELTEPILSRFDILQVVKDTVNPEIDEQLANFVVSSHIRSHPAFDPNMDVLKKVPTETGIDAKPIPQDLLRKYIHFAREKVFPRLQQMDEEKISRLYSDMRRESLATGSYPITVRHLESAIRLSEAFAKMQLSEFVRPSHIDKAIQVIIDSFVNAQKMSVKRSLSRTFAKYLI
Protein: Inorganic pyrophosphatase TTM2 (EC 3.6.1.1) (Triphosphate tunnel metalloenzyme 2) (AtTTM2) (Q9C664)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Exhibits pyrophosphatase activity with stronger affinity for pyrophosphate (PPi), moderate affinity for ATP and ADP, and weak affinity for tripolyphosphate (PPPi). No activity observed toward uridine substrate. Negative regulator of the salicylic acid (SA)-mediated amplification of defense responses against both virulent and avirulent pathogens, including oomycetes (e.g. H.arabidopsidis) and bacteria (e.g. P.syringae). Represses systemic acquired resistance (SAR).
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:28733390}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Uridine nucleosidase 1
- Uridine 5'-monophosphate synthase
- UMP kinase
- Uracil phosphoribosyltransferase, chloroplastic
- dCMP deaminase
- Alkaline-phosphatase-like family protein
- Dihydroorotate dehydrogenase
- Cytidine deaminase 7
- Cytidine deaminase 2
- Cytidine deaminase 3
Sequence:
MGQDSNGIEFHQKRHGLLKDQVQLVKRRDSIRYEIVSIQDRLSFEKGFFAVIRACQLLSQKNDGIILVGVAGPSGAGKTVFTEKILNFLPSVAVISMDNYNDSSRIVDGNFDDPRLTDYDTLLKNLEDLKEGKQVEVPIYDFKSSSRVGYRTLDVPPSRIVIIEGIYALSEKLRPLLDLRVSVTGGVHFDLVKRVLRDIQRAGQQPEEIIHQISETVYPMYKAFIEPDLQTAQIKIINKFNPFTGFQSPTYILKSRKEVSVDQIKAVLSDGHTETKEETYDIYLLPPGEDPESCQSYLRMRNKDGKYSLMFEEWVTDTPFVISPRITFEVSVRLLGGLMALGYTIATILKRNSHVFATDKVFVKIDWLEQLNRHYMQVQGKDRQLVQSTAEQLGLEGSFIPRTYIEQIQLEKLINEVMALPDDLKNKLSLDEDLVSSSSPKEALLRASADRVAMRNKNLKRGMSHSYSTQRDKNLSKLAGYSSSDRRYEERNHDSPANEGFMTLLSEQISSLNERMDEFTSRIEELNSKLSCNKNSPTQQSLSIQTEVCNGSAPTSYFISGLDNGCLTNSIMPHSSSSSQLAKDSPLMEEISTISRGQRQVMHQLDNLCNLMRESSAERSRLARTGSSNSGNRGRSSKSSFLSNVESNKLPLVLTVAICSIGIIVIKSYINKRQ
Protein: PtdIns3K complex I subunit atg38 (Autophagy-related protein 38) (Q05789)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Autophagy-related protein required for cytoplasm to vacuole transport (Cvt) and autophagy as a part of the autophagy-specific VPS34 PI3-kinase complex I. This complex is essential to recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-autophagosomal structure. ATG38 is required for the integrity of the active PI3-kinase complex I by maintaining an association between VPS15-VPS34 and ATG1P-VPS30 subcomplexes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Preautophagosomal structure membrane {ECO:0000269|PubMed:24165940}; Peripheral membrane protein {ECO:0000305|PubMed:24165940}. Note=Localization to the preautophagosomal structure requires ATG14. {ECO:0000269|PubMed:24165940}.
Interaction partners:
- Serine/threonine-protein kinase VPS15
- Vacuolar protein sorting-associated protein 30
- Phosphatidylinositol 3-kinase VPS34
- Autophagy-related protein 14
- Serine/threonine-protein kinase ATG1
- Autophagy-related protein 18
- Vacuolar protein sorting-associated protein 38
- Polyphosphoinositide phosphatase
- 1-phosphatidylinositol 3-phosphate 5-kinase FAB1
- Vacuolar segregation protein 7
Sequence:
MSTLAEVYTIIEDAEQECRKGDFTNAKAKYQEAIEVLGPQNENLSQNKLSSDVTQAIDLLKQDITAKIQELELLIEKQSSEENNIGMVNNNMLIGSVILNNKSPINGISNARNWDNPAYQDTLSPINDPLLMSILNRLQFNLNNDIQLKTEGGKNSKNSEMKINLRLEQFKKELVLYEQKKFKEYGMKIDEITKENKKLANEIGRLRERWDSLVESAKQRRDKQKN