wanglab/gogpt-training-data huggingface dataset:
Protein: Peroxisomal biogenesis factor 2 (EC 2.3.2.36) (Peroxin-2) (P32800)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: E3 ubiquitin-protein ligase component of a retrotranslocation channel required for peroxisome organization by mediating export of the PEX5 receptor from peroxisomes to the cytosol, thereby promoting PEX5 recycling. The retrotranslocation channel is composed of PEX2, PEX10 and PEX12; each subunit contributing transmembrane segments that coassemble into an open channel that specifically allows the passage of PEX5 through the peroxisomal membrane. PEX2 also regulates peroxisome organization by acting as a E3 ubiquitin-protein ligase. PEX2 ubiquitinates PEX5 during its passage through the retrotranslocation channel: catalyzes monoubiquitination of PEX5 at 'Cys-6', a modification that acts as a signal for PEX5 extraction into the cytosol.
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:12876220, ECO:0000269|PubMed:35768507}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Peroxisome assembly protein 12
- Peroxisome biogenesis factor 10
- Peroxisomal membrane protein PEX13
- Peroxisomal biogenesis factor 8
- Peroxisomal membrane protein PEX14
- Peroxisomal targeting signal receptor
- Peroxisomal membrane protein PEX17
- Peroxisomal membrane protein import receptor PEX19
- Peroxisomal membrane protein PMP27
- Ubiquitin-conjugating enzyme E2-21 kDa
Sequence:
MSRVAQLDSIALDKELYGQFWSEFNAAFNTSEHKEEWELALNTVVFMCATRFLPHYGSSCTYGSALSGVVFQCRKRTLYVVTVLAGYVWKKITHIIFNGPHCGNQMMWLKLYKWVNLLYHGCDVTNFLRFLAAEGPNARAFLSPLYRAFNVHSTRLIRDGSAIASEFYSNSVFAGLEYQNRQLLWNALLELFSNTLLTKRGLLTFVKKPPRSRSTTTYKTVCPRCGGFPTNPYQIACCRANYCYVCVVKALEWSMCDACGSSGRLTASPVY
Protein: Agglutinin-like protein N-terminal domain-containing protein (G8BJ59)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Secreted, cell wall {ECO:0000256|ARBA:ARBA00004191}.
Interaction partners:
- SPX domain-containing protein
- Ubiquitin-like domain-containing protein
- Glycerophosphodiester phosphodiesterase
- 60S ribosomal protein L21-A
- Large ribosomal subunit protein eL40 domain-containing protein
- Uncharacterized protein
- Large ribosomal subunit protein uL2 C-terminal domain-containing protein
- MPN domain-containing protein
- 60S ribosomal protein L16
- Zn
Sequence:
MVKHLQFVTILVAFTLTALTQAAEISNVFQSFDSLTWENGASYRYRTPAAPSWIAQLSWKILGSNVKPGDTFTLNMPCVFKFTTTQQSVDLDVGDTVYATCRFEPGDLVVAYSQLKCTASDNVKDSTDATGTVRFPFTFNVGGSAGVVDLQNSKCFTPGTNEVTFTDGDKKLTTTANFQGGSNTNPGTSTNNIVFNNRVVPSLNKQQLYLLGGTCPNGYRSGTLGITVSGGTLDCSSIHSAITNKLNGWFLPEVAEAISASTNCNGQSYTINYNNIPGGYRPFLDVLVQRPTGQVLRTNYINRYQCAGEIFVRDNSQSIKWGEYRNNEAGANGNEVVVTTSTWLGSTTALTTLPFNTEPGNTKTILVEVPIPTTTVTSSYTGYSTWTTTITATPGETATVLEWDPITPTSSSEPPSSSEPPSSSEPPSSSEPPSSSEPPSSSEPPSSSEPPSSSEPPSSSESESSSEPPSSSEPPSSSEPPSSSESESSSEPPSSSEPESSSEPPSSSEPPSSSEPESSSEPPSSSEPPSSSGPPSSSEPPSSSEPPSSSESESSSEPPSSSEPPSSSEPPSSSEPPSSSEPESSSEPPSSSGPPSSSEPPSSSEPPSSSEPPSSSEPPSSSESESSSEPPSSSETESSTEPPSSSSDTDFSSSSQVSSNDHSSSSITPPYQNSTSPTGPSSVPPSSESTTTPTDLPTTESTTDISSPSSESAITSPTTTPTTTDNGNGGENTPTTTDNGNGGENTPTTTDNGNGGENTPTTTDNGNGGENTPTTTDNGNGGENTPTTTDNGNGGENTPTTTDNGNGGENTPTTTDNGNGGENTPTTTDNGNGGENTPTTTDNGNGGENTPTTTDNGNGGENTNTPTNTGASTPSNPTTSSANTIDSQSTASSTNPPENGGNGGNSGNNGNGGNNGNNGNEGNGSGNGSGEGSGNGSGNGSGNGSGNGSGNGSGNGSGNGSGNGSGEGSGEGSGEGSGNGSGEGSGEGSGEGSGNGSGEGSGNGSGEGSGNGSGNGSGNGSGNGSGNGSGNGSGNGSGNGSGEGSGEGSGEGSGNGSGNGSGNGSGNGSGNGSGNGSGEGSGEGSGEGSGEGSGNGSGNGSGNGSGNESGESLSQSATTDTTSPAVSSYEGSGSIQRVSTLLTSLFVAISISF
Protein: 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoA reductase) (EC 1.1.1.34) (Q01237)
Organism: Mus musculus (Mouse)
Function: Catalyzes the conversion of (3S)-hydroxy-3-methylglutaryl-CoA (HMG-CoA) to mevalonic acid, the rate-limiting step in the synthesis of cholesterol and other isoprenoids, thus plays a critical role in cellular cholesterol homeostasis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P04035}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P00347}. Peroxisome membrane {ECO:0000250|UniProtKB:P04035}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P00347}.
Interaction partners:
- Hydroxymethylglutaryl-CoA synthase, cytoplasmic
- Hydroxymethylglutaryl-CoA synthase, mitochondrial
- Insulin-induced gene 1 protein
- Mevalonate kinase
- Squalene monooxygenase
- Lanosterol 14-alpha demethylase
- 5'-AMP-activated protein kinase catalytic subunit alpha-1
- Insulin-induced gene 2 protein
- 5'-AMP-activated protein kinase catalytic subunit alpha-2
- Squalene synthase
Sequence:
MLSRLFRMHGLFVASHPWEVIVGTVTLTICMMSMNMFTGNNKICGWNYECPKFEEDVLSSDIIILTITRCIAILYIYFQFQNLRQLGSKYILGIAGLFTIFSSFVFSTVVIHFLDKELTGLNEALPFFLLLIDLSRASALAKFALSSNSQDEVRENIARGMAILGPTFTLDALVECLVIGVGTMSGVRQLEIMCCFGCMSVLANYFVFMTFFPACVSLVLELSRESREGRPIWQLSHFARVLEEEENKPNPVTQRVKMIMSLGLVLVHAHSRWIADPSPQNSTAEQAKVSLGLDEDVSKRIEPSVSLWQFYLSKMISMDIEQVITLSLAFLLAVKYIFFEQAETESTLSLKNPITSPVVTSKKAQDNCCRREPLLVRRNQKLSSVEEDPGANQERKVEVIKPLVVEAETTSRATFVLGASVASPPSALGTQEPGIELPIEPRPNEECLQILENAEKGAKFLSDAEIIQLVNAKHIPAYKLETLMETHERGVSIRRQLLSTKLAEPSSLQYLPYRDYNYSLVMGACCENVIGYMPIPVGVAGPLCLDGKEYQVPMATTEGCLVASTNRGCRAISLGGGASSRVLADGMTRGPVVRLPRACDSAEVKTWLETPEGFAVIKEAFDSTSRFARLQKLHVTMAGRNLYIRFQSRTGDAMGMNMISKGTEKALLKLQEFFPDMQILAVSGNYCTDKKPAAINWIEGRGKTVVCEAVIPAKVVREVLKTTTEAMVDVNINKNLVGSAMAGSIGGYNAHAANIVTAIYIACGQDAAQNVGSSNCITLMEASGPTNEDLYISCTMPSIEIGTVGGGTNLLPQQACLQMLGVQGACKDNPGENARQLARIVCGTVMAGELSLMAALAAGHLVRSHMVHNRSKINLQDLQGTCTKKAA
Protein: Phosphoglucomutase 2 (PGM 2) (EC 5.4.2.2) (D-glucose-1,6-diphosphate:D-glucose-1-phosphate phosphotransferase) (Glucose phosphomutase 2) (P37012)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Major phosphoglucomutase isozyme that catalyzes the reversible interconversion of glucose 1-phosphate and glucose 6-phosphate. Constitutes about 80-90% of the phosphoglucomutase activity in the cell. Key enzyme in hexose metabolism. The forward reaction is an essential step in the energy metabolism of galactose since the product of the galactose pathway enzymes in yeast is glucose 1-phosphate. The reverse reaction is an essential step for biosynthesis when carbon sources other than galactose are the energy source because glucose 1-phosphate is the starting point for the synthesis of UDP-glucose, which acts as a precursor for the synthesis of oligosaccharides and trehalose.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:8385141}.
Interaction partners:
- UTP--glucose-1-phosphate uridylyltransferase
- Glycogen phosphorylase
- Phosphoribomutase
- Glucose-6-phosphate isomerase
- Hexokinase-1
- Glucokinase-1
- Glycogen debranching enzyme
- Phosphoglucomutase 1
- Glycogen [starch] synthase isoform 2
- Probable UTP--glucose-1-phosphate uridylyltransferase
Sequence:
MSFQIETVPTKPYEDQKPGTSGLRKKTKVFKDEPNYTENFIQSIMEAIPEGSKGATLVVGGDGRYYNDVILHKIAAIGAANGIKKLVIGQHGLLSTPAASHIMRTYEEKCTGGIILTASHNPGGPENDMGIKYNLSNGGPAPESVTNAIWEISKKLTSYKIIKDFPELDLGTIGKNKKYGPLLVDIIDITKDYVNFLKEIFDFDLIKKFIDNQRSTKNWKLLFDSMNGVTGPYGKAIFVDEFGLPADEVLQNWHPSPDFGGMHPDPNLTYASSLVKRVDREKIEFGAASDGDGDRNMIYGYGPSFVSPGDSVAIIAEYAAEIPYFAKQGIYGLARSFPTSGAIDRVAKAHGLNCYEVPTGWKFFCALFDAKKLSICGEESFGTGSNHVREKDGVWAIMAWLNILAIYNKHHPENEASIKTIQNEFWAKYGRTFFTRYDFEKVETEKANKIVDQLRAYVTKSGVVNSAFPADESLKVTDCGDFSYTDLDGSVSDHQGLYVKLSNGARFVLRLSGTGSSGATIRLYIEKYCDDKSQYQKTAEEYLKPIINSVIKFLNFKQVLGTEEPTVRT
Protein: Zinc finger protein 449 (Zinc finger and SCAN domain-containing protein 19) (Q6P9G9)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
Interaction partners:
Sequence:
MAVALGCAIQASLNQGSVFQEYDTDCEVFRQRFRQFQYREAAGPHEAFNKLWELCCQWLKPKMRSKEQILELLVLEQFLTILPTEIETWVREHCPENRERVVSLIEDLQRELEIPEQQVDMHDMLLEELAPVGTAHIPPTMHLESPALQVMGPAQEAPVAEAWIPQAGPPELNYGATGECQNFLDPGYPLPKLDMNFSLENREEPWVKELQDSKEMKQLLDSKIGFEIGIENEEDTSKQKKMETMYPFIVTLEGNALQGPILQKDYVQLENQWETPPEDLQTDLAKLVDQQNPTLGETPENSNLEEPLNPKPHKKKSPGEKPHRCPQCGKCFARKSQLTGHQRIHSGEEPHKCPECGKRFLRSSDLYRHQRLHTGERPYECTVCKKRFTRRSHLIGHQRTHSEEETYKCLECGKSFCHGSSLKRHLKTHTGEKPHRCHNCGKSFSRLTALTLHQRTHTEERPFKCNYCGKSFRQRPSLVIHLRIHTGEKPYKCTHCSKSFRQRAGLIMHQVTHFRGLI
Protein: Amino acid permease 5 (Amino acid transporter AAP5) (Q8GUM3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Amino acid-proton symporter. Stereospecific transporter with a broad specificity for glutamate and both neutral and basic amino acids. Reduced affinities for asparagine and valine. High affinity transport of the cationic amino acids arginine and lysine, but not of histidine.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Cationic amino acid transporter 6
- WAT1-related protein At4g01430
- WAT1-related protein At1g01070
- WAT1-related protein At2g39510
- WAT1-related protein At1g44800
- Cationic amino acid transporter 8
- WAT1-related protein At1g25270
- WAT1-related protein At2g40900
- Cationic amino acid transporter 9
- WAT1-related protein At1g09380
Sequence:
MVVQNVQDLDVLPKHSSDSFDDDGRPKRTGTVWTASAHIITAVIGSGVLSLAWAVAQIGWIGGPVAMLLFSFVTFYTSTLLCSCYRSGDSVTGKRNYTYMDAIHSNLGGIKVKVCGVVQYVNLFGTAIGYTIASAISLVAIQRTSCQQMNGPNDPCHVNGNVYMIAFGIVQIIFSQIPDFDQLWWLSIVAAVMSFAYSAIGLGLGVSKVVENKEIKGSLTGVTVGTVTLSGTVTSSQKIWRTFQSLGNIAFAYSYSMILIEIQDTVKSPPAEVNTMRKATFVSVAVTTVFYMLCGCVGYAAFGDNAPGNLLAHGGFRNPYWLLDIANLAIVIHLVGAYQVYCQPLFAFVEKEASRRFPESEFVTKEIKIQLFPGKPFNLNLFRLVWRTFFVMTTTLISMLMPFFNDVVGLLGAIGFWPLTVYFPVEMYIAQKNVPRWGTKWVCLQVLSVTCLFVSVAAAAGSVIGIVSDLKVYKPFQSEF
Protein: GINS subunit domain-containing protein (Q383N3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- DNA replication complex GINS protein SLD5
- DNA replication licensing factor MCM5
- DNA replication licensing factor MCM4
- Uncharacterized protein
- GINS subunit domain-containing protein
- Cell division cycle 45
- DNA replication licensing factor MCM3
- GINS subunit domain-containing protein
- DNA helicase
- DNA polymerase II subunit 2
Sequence:
MSAGSAASHPVASHAGNSRSGSFTMYHFASFAAMEVTVTIVPRFTMPRISTAFGGRYGPFTPNFPTDVPLWLALHIRQTDTCTIQPPPYVALPHLRQVLEREKENETTFEALPFYFFEVVKKLCEVSAAAEDVPHVAEVVRLVDEVRAVRRRKLQQSMSVFEAEGSPVFIPGIKLSNIVNHELQYLRTSFAIVLQQSADMKQRREQDIGGPIESVPTPIRTSGTALSYTPLSTAAAAEGRLLDYAATRSSDTHDSLSTSAAAEQAIFTPENTFTTDGTPSVADATETGTASMSEEISGPPVKKRRTLRQT
Protein: Probable NADPH:adrenodoxin oxidoreductase, mitochondrial (AR) (Adrenodoxin reductase) (EC 1.18.1.6) (Ferredoxin--NADP(+) reductase) (Ferredoxin reductase) (O59710)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Serves as the first electron transfer protein in all the mitochondrial P450 systems.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P48360}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- Glutamate synthase
- Heme A synthase-mitochondrial ferredoxin fusion protein
- Dihydroorotate dehydrogenase
- Uncharacterized FAD-binding protein C17H9.12c
- Protein isd11
- NADH-cytochrome b5 reductase 1
- Glutamine synthetase
- Probable electron transfer flavoprotein subunit beta
- Sulfite reductase subunit beta
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
Sequence:
MLSRFIKRTYSTQTSSPVVGIIGSGPAAFYTAHRLLRNDPNVKIDMFESRPVPFGLVRYGVAPDHPEVKHVEHKFSEIAESTQFRFLGNVNVGTDVSLRDLTKNYDCLVLAYGAAGDKRLGIPGEDLSGVYSAREVVGWYNSDPRNQNLELDLSQVEDAVVIGHGNVSLDVARILLSNPAQLSPTDINPLFLKSLERSNLKRLHIVGRRNIFSVSFTIKELRELFALSSAVFFAPSFNYSTKWMNETDASGLDRPRKRLLKLLVSEIQKAVSEKRVAPYSKDKKCWNLEFGLTPVEILGHKGNVENVRFQITDSIRTDAESKFTTIPAQLFIRSIGYKSMPLPGMKDVGVPFDDAKGIVKNVNGFVRPGIYTSGWVKHGPIGVIATTMMDAFATADTITKDWKSKKEFLKNSKLGWDGLKKNIKTPVIHWKDWKVIRNAEIERGLRHESLSEKFRSNEDMIKLIYPGKK
Protein: Nucleolar MIF4G domain-containing protein 1 (SGD1 homolog) (Q3UFM5)
Organism: Mus musculus (Mouse)
Function: Plays a role in targeting PPP1CA to the nucleolus.
Subcellular location: Nucleus, nucleolus {ECO:0000250}.
Interaction partners:
- Neuroguidin
- Probable ATP-dependent RNA helicase DDX10
- KRR1 small subunit processome component homolog
- WD repeat-containing protein 3
- RNA cytidine acetyltransferase
- Something about silencing protein 10
- Ribosomal RNA processing protein 36 homolog
- ESF1 homolog
- Nucleolar complex protein 4 homolog
- U3 small nucleolar RNA-interacting protein 2
Sequence:
MPRNVPEVNGVYRHGACELWCRAMAHALLKRSGVRRGLGGREGPLKRLRLAVEDFVRTTSESEACESRSAVARSRPGGRKSRKELRKEKRHLRKARRLQRTVGSGSGDQGGNVGLNDGPETRRPPTEVRPTPAKATATPAKASAPSTNTKASAAQPKAKAKGAPGKPGPATATARKRALLAANEEEDREIRKLERCLGLHKRKKKGDGSSVPLSFARDGLDYILGALECGSGGGLYESSEEEEEEKLETGQTVLESDLESNSKESEEDPDWQVLQEDQEDVNSKRRGEAESGTRGNKGTKKVRFAEVVEKSRSSSEDDIEQQESHSVESGEKYIPPRLRNEEVIDVHKKEELDRLKKHVKGLINRLSEPNMASISGQLEELYMAHSRKDMNDTLTTALMDACVTASAMPSRLMMEHVFLVSILHHTVGIEVGACFLEAVVKKFDAIYRDGGEGKELDNLFTMIAHLYNFHVVQSILIFDILKKLVGTFTEKDIELILLMLKNVGFALRKDDALSLKELITEAQTQASGAGNKFQDQNRVRFMLETMLALKNNDLRKIPGYNPEPVEKLKKLQRTLVRNAGSGSETRLRISWDGILNAEQTGRWWIVGSAWSGTPMIDNSHHIQLQKPLAGMASSKMLELARKQRMNTDVRRIIFCTLMTSEDFLDAFEKLLKLGLKDQQEREIVHILMDCCLQEKTYNPFYAFLASKFCDYERRFQMTFQFSIWDKFRDLENLPDTKFSNLVHLLAHLLRTKSLPLSVLKVVEFSELDKPRVHFLRRVLTALLMETEDDDLAVIFSRVSDNPKLGMLREGLKLFIGHFLLKHTQAHQSAEEASLLREKAGLASKSLQGKAILRM
Protein: Cell division protein SepF (O31728)
Organism: Bacillus subtilis (strain 168)
Function: Cell division protein that is part of the divisome complex and is recruited early to the Z-ring. Probably stimulates Z-ring formation, perhaps through the cross-linking of FtsZ protofilaments. Its function overlaps with FtsA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16420366, ECO:0000269|PubMed:16796675}. Note=Localizes to the division site, in a FtsZ-dependent manner.
Interaction partners:
- Cell division protein FtsZ
- Cell division protein FtsA
- Septation ring formation regulator EzrA
- Cell division protein ZapA
- Uncharacterized membrane protein YlmG
- Pyridoxal phosphate homeostasis protein
- Septum site-determining protein DivIVA
- Cell division protein FtsL
- Purine nucleoside phosphorylase YlmD
- Probable peptidoglycan glycosyltransferase FtsW
Sequence:
MSMKNKLKNFFSMEDEEYEYEYIETERESHEEHEQKEKPAYNGNKPAGKQNVVSLQSVQKSSKVVLSEPRVYAEAQEIADHLKNRRAVVVNLQRIQHDQAKRIVDFLSGTVYAIGGDIQRIGSDIFLCTPDNVDVSGTISELISEDEHQRW
Protein: DSec61alpha (LD29847p) (Sec61 alpha subunit, isoform A) (Sec61 alpha subunit, isoform B) (Q8STG9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}. Membrane {ECO:0000256|RuleBase:RU003484}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU003484}.
Interaction partners:
- Small ribosomal subunit protein uS3
- 40S ribosomal protein S15
- Elongation factor Ts, mitochondrial
- RE14391p
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein uL29
- GM03767p
- FI01658p
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein bL17m
Sequence:
MGIKFLEVIKPFCSILPEIAKPERKIQFREKVLWTAITLFIFLVCCQIPLFGIMSSDSADPFYWIRVILASNRGTLMELGISPIVTSGLIMQLLAGAKIIEVGDTPKDRALFNGAQKLFGMVITIGQAIVYVMTGMYGDPSEIGAGVCLLIIIQLFAAGLIVLLLDELLQKGYGLGSGISLFIATNICETIVWKAFSPTTVTTGRGTEFEGAVIALFHLMATRNDKVRALREAFYRQNLPNLMNLLATVLVFAVVIYFQGFRVDLPIKSARYRGQYSSYPIKLFYTSNIPIILQSALVSNLYVISQMLAVKFQGNFFINLLGVWADVGGGGPARSYPIGGLCYYLSPPESVGHILTDPIHALLYIVFMLGSCAFFSKTWIDVSGSSAKDVAKQLKEQHMVMRGHRENSMIHELNRYIPTAAAFGGLCIGALSVMADFLGAIGSGTGILLAVTIIYQYFEIFVKEQSEMGGMGTLLF
Protein: Imidazoleglycerol-phosphate dehydratase (EC 4.2.1.19) (Q59LL5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Imidazole glycerol phosphate synthase hisHF
- Histidine biosynthesis trifunctional protein
- histidinol-phosphate transaminase
- ATP phosphoribosyltransferase
- 1-
- N-
- 3-isopropylmalate dehydrogenase
- Orotidine 5'-phosphate decarboxylase
- Phosphoribosylaminoimidazole carboxylase
- phosphoserine phosphatase
Sequence:
MSREALINRITNETKIQIALNLDGGKLELKESIFPNQSIIIDEHHAKQVSGSQYINVQTGIGFLDHMIHALAKHSGWSLIVECIGDLHIDDHHTAEDVGISLGMAFKQALGQIKGVKRFGHGFAPLDEALSRAVVDLSNRPFAVIELGLKREKIGDLSTEMIPHVLESFAGAAGITIHVDCLRGFNDHHRAESAFKALAIAIKEAISKTGKNDIPSTKGVLS
Protein: 6-carboxyhexanoate--CoA ligase (EC 6.2.1.14) (Pimeloyl-CoA synthase) (P22822)
Organism: Lysinibacillus sphaericus (Bacillus sphaericus)
Function: Catalyzes the transformation of pimelate into pimeloyl-CoA with concomitant hydrolysis of ATP to AMP.
Interaction partners:
Sequence:
MLETCYSIRMRAAEKNLEGGEKHISGGERIGSEFQIEPIVKQLLNKARNHSRGDADFIQITVEKLTGDQILYMPPLEITTIDESSIERAHKEARSILTSVGVSKQAQNVAFHLLASNQNLRGAILLHSQTGLRLDNRGLKGVRVSRIDWQDADVGYNERVREALALATKVANSPYTIAELCWSDDPEYVTGYVSNHEIGYVRITPLKREGCESGGRIFFVSDEVELESYIHYLEREPILIRGHLK
Protein: Octaprenyl diphosphate synthase (EC 2.5.1.90) (All-trans-octaprenyl-diphosphate synthase) (Octaprenyl pyrophosphate synthase) (OPP synthase) (P0AD57)
Organism: Escherichia coli (strain K12)
Function: Supplies octaprenyl diphosphate, the precursor for the side chain of the isoprenoid quinones ubiquinone and menaquinone.
Interaction partners:
- Ditrans,polycis-undecaprenyl-diphosphate synthase
- 4-hydroxybenzoate octaprenyltransferase
- Farnesyl diphosphate synthase
- 1,4-dihydroxy-2-naphthoate octaprenyltransferase
Sequence:
MNLEKINELTAQDMAGVNAAILEQLNSDVQLINQLGYYIVSGGGKRIRPMIAVLAARAVGYEGNAHVTIAALIEFIHTATLLHDDVVDESDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITEENYMRVIYSKTARLFEAAAQCSGILAGCTPEEEKGLQDYGRYLGTAFQLIDDLLDYNADGEQLGKNVGDDLNEGKPTLPLLHAMHHGTPEQAQMIRTAIEQGNGRHLLEPVLEAMNACGSLEWTRQRAEEEADKAIAALQVLPDTPWREALIGLAHIAVQRDR
Protein: Receptor-type tyrosine-protein phosphatase F (EC 3.1.3.48) (H9CWQ2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MVPQTRQGSARHGATSLLLLLLCLAVPIHADSMPSFVKTPEDQTGISGGVASFVCQAVGEPKPRITWMKKGKKVSSQRFEVIEFDDGSGSVLRIQPLRTHRDEAIYECTATNSVGEINTSAKLTVLEEDQIPHGFPTIDMGPQLKVVERTRTATMLCAASGNPDPEISWFKDFLPVDINSSNGRIKQLRSGALQIENSEESDQGKYECVAVNSAGTRYSAPANLYVRVRRVPPRFSIPPTNHEVMPGGSVNLTCVAVGAPMPYVKWMKGEQELTKEEEMPIGRNVLELTNIRQSGNYTCVAISSLGMIDTTAQITVKALPRPPASLIVTETTATSVTLTWDSGNPEPVSYYVIQYRSKISDNGFQEVDGVASTRYSIGGLSPYSEYEFRVMAVNNIGRGPPSGMVETRTSEQAPSSPPLRVQARMLSATTMLVQWEPPEEPNGQIRGYRVYYTSDLHFPLSTWQKHNTEDSSLTTISGLVPDITYGLRVLAFTSVGDGPPSDILQVKTQQGVPAQPTGFEAEAELDTRIMLSWLWPVQDQITKYELTYWEADSDNKHHVIFDPAGSYAIDSLKPDTLYKFSLAARSEMGLGVYTQPIEARTAQSAPSAPPQEVHLISLSSSSIKVSWVAPPAASRHGSIVRYSLAYQAVSGEDQERHEVKDIPADVSSYVLEGLEKWTEYTVWVKAHTDVGPGPESGSTRIRTQEDVPGAPPRRVEVDNINSTALRVSWKPPLQQKQHGHIRGYQVVYSRLENGEPRGQPIILDVALPEAQEAVISGLLPETTYSVTVAAYTTKGDGARSKAKVVTTTGAVPGKPTMIISTTIGNTALIQWQPPKEMVGELMGYRLRYKREEEDIYTVRDFRRTDDHFTVTGLHKGATYIFKLCAKNRAGNGEEYSKEISTPEDVPSSYPQNLKVVGLTTTTTKLAWDPPPLPERNGKIVRYVVVYRDINSHQNQTNGTADTEMTIQGLKPDTTYDIRVRAFTGKGGGPISPSIQSRTMSTSMPEFTKNFGVKAVMKTSVLLTWEVPETYKSQVPFKILYNQQSVEVQGDLKRKLITRLQPDTDYSFVLMSRGNSAGGLQQQVSIRTAPDLFTTKPAHQKLDPEEGGKLAITLPEVHNSALVRWFYIVVVPVTPSTLRHWENPEDIDLDELMGNNRDAAVRRRRRQTQDFLRPYIAAKLESLPERFVLGDEKTYSNYYNKPLPGQQQYRTFILAALKDRDSTFTVSPFSEPMMVKLHSGMSRHVEDPEMLWVMGPVLAVVLIIIIVIAILLFKRKRTSPSAKDEHSAGVKDHLLAHSSDPVEMRRLNYQTQGMREHPPVSVCALADHIERLRANDSLRFSQEYESVDPGQQFTWENSNLEVNKPKNRYANVIAYDHSRVVLTPVDGVPGSDYINGNYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTSTIVMMTRLEEKSRVKCDQYWPSRGTETYGMIQVSMLDTVELATYSVRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKSVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAATCGNTEVPARSLYTHIQKLTQAPPGDTVTAMELEFKKLANSKAHTSRFISASLPCNKFKNRLVNIMPFESSRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLSETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTIKTLRTQRPAMVQTEDQYQLCYRAALEYLGSFDHYAT
Protein: CTP synthase 1 (EC 6.3.4.2) (CTP synthetase 1) (UTP--ammonia ligase 1) (Q6PEI7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: This enzyme is involved in the de novo synthesis of CTP, a precursor of DNA, RNA and phospholipids. Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as a source of nitrogen.
Interaction partners:
- Nucleoside diphosphate kinase 6
- Ectonucleoside triphosphate diphosphohydrolase 8
- Adenylate kinase 9
- Ectonucleoside triphosphate diphosphohydrolase 1
- Bis
- Nucleoside diphosphate kinase
- Nucleoside diphosphate kinase.
- Nucleoside diphosphate kinase 7
- Nucleoside diphosphate kinase 3
- Nucleoside diphosphate kinase
Sequence:
MKYILVTGGVISGIGKGIIASSVGTILKSCGLHVTAIKIDPYINIDAGTFSPYEHGEVFVLDDGGEVDLDLGNYERFLDIRLTKDNNLTTGKIYQSVINKERRGDYLGKTVQVVPHITDAIQEWVMRQAKIPVDDDDVEPQVCVIELGGTVGDIESMPFVEAFRQFQFKVKRENFCNIHVSLVPQPSATGEQKTKPTQNSVRELRGLGLSPDLIMCRCSTPLDNSVKEKISMFCHVEPEQVICVHDVSSIYRVPLLLEDQGVVGYFCRRLNLPIENRPRKMLAKWKEMSDRSDRLLEQCSIALVGKYTKFSDSYASVIKALEHSALAISHKLEVKYVDSADLEPSMLQEEPVKYHEAWQKLCSSDGILVPGGFGVRGTEGKIQAINWARKQKKPFLGVCLGMQLAVCEFARNMLDWTDANSTEFDPETKHPVVIDMPEHNPGQMGGTMRLGKRRTIFKNKSSILRKLYGDVDYVEERHRHRFEVNPELKHHFEEKGFRFVGQDVEGERMEVIEMDDHPYFVGVQYHPEFTSRPIKPSPPYLGLLLAAAGRLQSYLQKGCRLSPRDAYSDRSGSSSPDLEIADLKLRSIAQE
Protein: Growth hormone receptor (Q0R5T9)
Organism: Bos taurus (Bovine)
Interaction partners:
Sequence:
EGKLEEVNTILAIHDNYKHEFYNDDSWVEFIELDIDDPDEKTEGSDTDRLLSNDHEKSLNIFGAKDDDSGRTSCYEPDILEADFHVSDMCDGTSEVAQPQRLKGEADISCLDQKNQNNSPSNDAAPASQQPSVILVEENKPRPLLIGGTESTHQAVHTQLSNPSSLANIDFYAQVSDITPAGNVVLSPGQKNKTGNPQCDTHPEVVTPCQANFIVDNAYFCEVDTKKYIALAPHVEAESHVEPSFNQEDIYITTESLTTTAGRSGTAEHVPSSEIPVPDYTSIHIVQSPQGLVLNATALP
Protein: Occludin (Q6P6T5)
Organism: Rattus norvegicus (Rat)
Function: May play a role in the formation and regulation of the tight junction (TJ) paracellular permeability barrier. May be involved in the organization of actin in endothelial cells.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q16625}; Multi-pass membrane protein {ECO:0000255}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q16625}.
Interaction partners:
- Claudin-1
- Tight junction protein ZO-1
- Tight junction protein 2
- Junctional adhesion molecule A
- Claudin-5
- Claudin-3
- Endothelial cell-selective adhesion molecule
- Claudin
- Cadherin-1
- Claudin
Sequence:
MSVRPFESPPPYRPDEFKPNHYAPSNDMYGGEMHVRPMLSQPAYSFYPEDEILHFYKWTSPPGVIRILSMLVIVMCIAVFACVASTLAWDRAYGTGIFGGSMNYPYGSGFGSYGGGFGGYGYGYGYGYGGYTDPRAAKGFLLAMAAFCFIASLVIFVTSVIRSGMSRTRRYYLIVIIVSAILGIMVFIATIVYIMGVNPTAQASGSMYGSQIYTICSQFYTPGGTGLYVDQYLYHYCVVDPQEAIAIVLGFMIIVAFALIIVFAVKTRRKMDRYDKSNILWDKEHIYDEQPPNVEEWVKNVSAGTQDMPPPPSDYAERVDSPMAYSSNGKVNGKRSYPDSLYKSPPLVPEVAQEIPLTLSVDDFRQPRYSSNDNLETPSKRTPTKGKAGKAKRTDPDHYETDYTTGGESCDELEEDWLREYPPITSDQQRQLYKRNFDAGLQEYKSLLAELDEVNKELSRLDRELDDYREESEEYMAAADEYNRLKQVKGSADYKSKKNYCKQLKSKLSHIKRMVGDYDRRKT
Protein: Protein MMF1, mitochondrial (Isoleucine biosynthesis and maintenance of intact mitochondria 1) (Maintenance of mitochondrial function 1) (P40185)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Plays a role in the maintenance of mitochondrial DNA.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:11003673, ECO:0000269|PubMed:11442631}.
Interaction partners:
- Catabolic L-serine/threonine dehydratase
Sequence:
MFLRNSVLRTAPVLRRGITTLTPVSTKLAPPAAASYSQAMKANNFVYVSGQIPYTPDNKPVQGSISEKAEQVFQNVKNILAESNSSLDNIVKVNVFLADMKNFAEFNSVYAKHFHTHKPARSCVGVASLPLNVDLEMEVIAVEKN
Protein: Vasoactive intestinal peptide receptor 2 (Vasoactive intestinal polypeptide receptor 2 precursor) (Vasoactive intestingal polypeptide receptor type 2) (A7UH65)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MSLVNCLVLLIVWHAHSVNGRHPNCQFLYELQMAEKECLGDLADEPLLHTEGCRGMWDNFSCWHHADVGKVVVNNCPAALKNLFTRDGIISRNCTTEGWSNVYPSIDSVCFAPTNTNTTMYVFYTVMKTLYTLGHSLSLIALITGSTILCLFRKLHCTRNYIHLNLFFSFILRAIAVLVKDAILFSHENGECTVQPSLMGCKVSLVILNYFIMANFYWLLVEGLYLHTLLMVIFSENRHFIIYLLIGWGFPTVFVIPWIVCRIYLEDTGCWERIDNPIPWRVINWPIMASVILNFILFISIIRILVQKLRCPDVGGNDQSQYRRLAKSTLLLIPLFGVHYIVFVYIIDGNGERENYKIFFDLGLGSFQGLVVAILYCFLNSEVQSELKRKWRSLRLKRYIGRDYRLHSSSISRNGTENMAQFQRNTRAQSFLQTETTVV