wanglab/gogpt-training-data huggingface dataset:
Protein: Ornithine transcarbamylase, chloroplastic (OTCase) (EC 2.1.3.3) (Ornithine carbamoyltransferase, chloroplastic) (O50039)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Argininosuccinate synthase, chloroplastic
- Carbamoyl phosphate synthase arginine-specific large chain, chloroplastic
- Argininosuccinate lyase, chloroplastic
- Arginine biosynthesis bifunctional protein ArgJ
- Arginase 1, mitochondrial
- Arginase 2, chloroplastic/mitochondrial
- Carbamoyl phosphate synthase small chain, chloroplastic
- Probable N-acetyl-gamma-glutamyl-phosphate reductase, chloroplastic
- Acetylornithine aminotransferase, chloroplastic/mitochondrial
- At1g44820
Sequence:
MAAAMASHVSTARSPALSFSSSSSSFFPGTTLRRFSAVSLPSPALPRLRVSCQASSVTSPSSPSDVKGKSDLKDFLAIDDFDTATIKTILDKASEVKALLKSGERNYLPFKGKSMSMIFAKPSMRTRVSFETGFFLLGGHALYLGPNDIQMGKREETRDVARVLSRYNDIIMARVFAHQDILDLANYSSVPVVNGLTDHNHPCQIMADALTMIEHIGQVEGTKVVYVGDGNNMVHSWLELASVIPFHFVCACPKGYEPDKERVSKAKQAGLSKIEITNDPKEAVIGADVVYSDVWASMGQKDEAEARRKAFQGFQVDEALMKLAGQKAYFMHCLPAERGVEVTNGVVEAPYSIVFPQAENRMHAQNAIMLHLLGF
Protein: Cell wall mannoprotein PIR3 (Covalently-linked cell wall protein 8) (Protein with internal repeats 3) (Q03180)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the outer cell wall layer. Required for stability of the cell wall and for optimal growth. Required for resistance against several antifungal and cell wall-perturbing agents.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:10407261, ECO:0000269|PubMed:15781460, ECO:0000269|PubMed:9192695}. Note=Covalently attached to the cell wall.
Interaction partners:
- Cell wall mannoprotein PST1
- Cell wall mannoprotein CIS3
- Cell wall protein CWP1
- Cell wall protein SED1
Sequence:
MQYKKPLVVSALAATSLAAYAPKDPWSTLTPSATYKGGITDYSSSFGIAIEAVATSASSVASSKAKRAASQIGDGQVQAATTTAAVSKKSTAAAVSQITDGQVQAAKSTAAAVSQITDGQVQAAKSTAAAVSQITDGQVQAAKSTAAAVSQITDGQVQAAKSTAAAASQISDGQVQATTSTKAAASQITDGQIQASKTTSGASQVSDGQVQATAEVKDANDPVDVVSCNNNSTLSMSLSKGILTDRKGRIGSIVANRQFQFDGPPPQAGAIYAAGWSITPEGNLALGDQDTFYQCLSGDFYNLYDKHIGSQCHEVYLQAIDLIDC
Protein: Possible 23S rRNA methyltransferase TsnR (P94978)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Large ribosomal subunit protein bL20
- Ribosomal silencing factor RsfS
- Translation initiation factor IF-3
- Large ribosomal subunit protein bL35
- Large ribosomal subunit protein bL17
- Large ribosomal subunit protein uL15
- Large ribosomal subunit protein bL21
- Large ribosomal subunit protein uL24
- Phenylalanine--tRNA ligase beta subunit
- Large ribosomal subunit protein uL13
Sequence:
MLTERSARVATAVKLHRHVGRRRAGRFLAEGPNLVAAALARGLVREVFVTEVAARRHELLLAAHEASVHLVTERAAKALSDTVTPAGLVAVCDLPATRLEDVLAGSPQLIAVTVEIREPGNAGTVIRIADAMGAAAVILAGRSVDPYNGKCLRASTGSIFAIPVVVAPDVGAAIADLRAAGLQVLATAVDGEMALDDADRLLAEPTAWLFGPEAHGLSAEIAALADHRVHILMSGGAESLNVAAAAAICLYESARALGRR
Protein: GDSL-lipase protein (Q08ET5)
Organism: Capsicum annuum (Capsicum pepper)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MMMGARELVRKWIVMYVVVLLGLNLWGYYGVNAQQVPCYFIFGDSLVDNGNNNNIQSLARANYLPYGIDYPGGPTGRFSNGKTTVDVIAELLGFEDYIPPYADARGEDILKGVNYASAAAGIRDETGQQLGARIPFGGQVNNYRDTVQQVVQILGNEDSAATYLSKCVYPIGLGSNDYLNNYFMPMYYSTGRQYNPEQYADILIQQYTQHLKTLYDYGARKFVLIGVGQIGCSPNALAQNSADGRTCAQNINAANQLFNNRLRGLVDEFNGNTPDAKFIYINAYDIFQDLIDNPSAFGFRVTNAGCCGVGRNNGQITCLPLQNPCPNRDEYLFWDAFHPGEAANTIVGRRSYRAERSSDAYPFDIQHLAQL
Protein: Sporulation protein SPS18 (Sporulation-specific protein SPX18) (P32572)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Peroxisomal 2,4-dienoyl-CoA reductase SPS19 [
- ADP-ribosylation factor 1
- ADP-ribosylation factor GTPase-activating protein GLO3
Sequence:
MRLFENSKDMENRKRLLRAKKAAGNNNCFECKSVNPQFVSCSFGIFICVNCANLLRGMGTNIFCVKSITMDNFEEKDVRRVEKSGNNRFGSFLSKNGILQNGIPLREKYDNLFAKSYKRRLANEVRSNDINRNMYLGFNNFQQYTNGATSQIRDRTLREISNNSNASEGAEFVLPEKVLGSDNFQDCERFPACLSSERNLDENNVTSATSTLTIEKFQNDPIGTISRSWQLLSDALYKSYEDFKGSVVQPTIENIQQRNLPNDIKRSFVHFNEKLHETPHLPSPVFSCFTGGDILPPEFN
Protein: ATP-dependent translocase ABCB1 (ATP-binding cassette sub-family B member 1A) (MDR1A) (Multidrug resistance protein 1A) (EC 7.6.2.2) (Multidrug resistance protein 3) (P-glycoprotein 3) (Phospholipid transporter ABCB1) (EC 7.6.2.1) (P21447)
Organism: Mus musculus (Mouse)
Function: Translocates drugs and phospholipids across the membrane. Catalyzes the flop of phospholipids from the cytoplasmic to the exoplasmic leaflet of the apical membrane. Participates mainly to the flop of phosphatidylcholine, phosphatidylethanolamine, beta-D-glucosylceramides and sphingomyelins. Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P08183}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. Apical cell membrane {ECO:0000269|PubMed:8898203}. Cytoplasm {ECO:0000250|UniProtKB:P08183}. Note=ABCB1 localization is influenced by C1orf115 expression levels (plasma membrane versus cytoplasm). {ECO:0000250|UniProtKB:P08183}.
Interaction partners:
- ATP-dependent translocase ABCB1
- Phosphatidylcholine translocator ABCB4
- Occludin
- Peptidyl-prolyl cis-trans isomerase G
- Cytochrome P450 3A11
- Cytochrome P450 3A
- Nuclear receptor subfamily 1 group I member 2
- Bile acid receptor
- Solute carrier organic anion transporter family member 1A6
Sequence:
MELEEDLKGRADKNFSKMGKKSKKEKKEKKPAVSVLTMFRYAGWLDRLYMLVGTLAAIIHGVALPLMMLIFGDMTDSFASVGNVSKNSTNMSEADKRAMFAKLEEEMTTYAYYYTGIGAGVLIVAYIQVSFWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITANISMGAAFLLIYASYALAFWYGTSLVISKEYSIGQVLTVFFSVLIGAFSVGQASPNIEAFANARGAAYEVFKIIDNKPSIDSFSKSGHKPDNIQGNLEFKNIHFSYPSRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMTQTAGNEIELGNEACKSKDEIDNLDMSSKDSGSSLIRRRSTRKSICGPHDQDRKLSTKEALDEDVPPASFWRILKLNSTEWPYFVVGIFCAIINGGLQPAFSVIFSKVVGVFTNGGPPETQRQNSNLFSLLFLILGIISFITFFLQGFTFGKAGEILTKRLRYMVFKSMLRQDVSWFDDPKNTTGALTTRLANDAAQVKGATGSRLAVIFQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTREQKFETMYAQSLQIPYRNAMKKAHVFGITFSFTQAMMYFSYAACFRFGAYLVTQQLMTFENVLLVFSAIVFGAMAVGQVSSFAPDYAKATVSASHIIRIIEKTPEIDSYSTQGLKPNMLEGNVQFSGVVFNYPTRPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSRVVSYEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGKVKEHGTHQQLLAQKGIYFSMVSVQAGAKRS
Protein: Solute carrier family 35 member E2A (P0CK97)
Organism: Homo sapiens (Human)
Function: Putative transporter.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MSSSVKTPALEELVPGSEEKPKGRSPLSWGSLFGHRSEKIVFAKSDGGTDENVLTVTITETTVIESDLGVWSSRALLYLTLWFFFSFCTLFLNKYILSLLGGEPSMLGAVQMLSTTVIGCVKTLVPCCLYQHKARLSYPPNFLMTMLFVGLMRFATVVLGLVSLKNVAVSFAETVKSSAPIFTVIMSRMILGEYTGRPSDREEREELQLQPGRGAAASDRRSPVPPSERHGVRPHGENLPGDFQVPQALHRVALSMALPCPMLPAS
Protein: SRP-independent targeting protein 2 (Late endosome and vacuole interface protein 10) (Q99382)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions in the SND pathway, a SRP (signal recognition particle) and GET (guided entry of tail-anchored proteins) independent pathway for targeting a broad range of substrate proteins to the endoplasmic reticulum. SND functions in parallel to GET in targeting proteins with downstream hydrophobic motifs. Involved in vacuolar processing and morphology.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:27905431}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Autophagy-related protein 9
- SRP-independent targeting protein 3
- Golgi to ER traffic protein 1
- ATPase GET3
- SRP-independent targeting protein 1
- Pachytene arrest protein SAE3
- Golgi to ER traffic protein 2
- Golgi to ER traffic protein 4
- Protein transport protein SEC61
- Protein-toxin resistance protein KTD1
Sequence:
MAGKAGRKQASSNAKIIQGLYKQVSLFLGMAIVRLFISRKVTIGQWIKLVALNVPMFVALYIIVLSGKPKYDGNRVVKQGIDLNDNTNLISYFFDLIYLSLFGNIGIIAFRTFKFWWCLLLCPIYAGYKLYGLKNMFMPGAQQTQADNRSKNANEGQSKSKRQMKRERRGETDSKIKYKYR
Protein: Presenilin-2 (PS-2) (Zf-PS2) (EC 3.4.23.-) (Pre2) (Q90ZE4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Probable catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Gamma-secretase subunit PEN-2
- Gamma-secretase subunit Aph-1b
- Ncstrn_small domain-containing protein.
- Zgc:114200.
- Presenilin-1
- Neurogenic locus notch homolog protein 1
- Amyloid beta
- Notch receptor 1b.
- Apolipoprotein Eb
- Amyloid beta
Sequence:
MNTSDSEEDSYNERSALVQSESPTVPSYNQDNAMSLPQDTDSKRSGAVRSRSASGSGDAGPVDRERADTPDGEEEELTLKYGAKHVIMLFIPVTLCMVVVVATIKSVSFYTEKSGQRLIYTPFEEDPNSVGQRLLNSVLNTLVMISVIVFMTIILVLLYKYRCYKFIHGWLILSSLMLLFWFSFMYLGEVFKTYNVAMDYPTLLMIIWNFGVVGMICIHWKGPLRLQQAYLIVISALMALIFIKYLPEWSAWVILGAISIYDLIAVLCPKGPLRMLVETAQERNEPIFPALIYSSAMVWMVGMADSNNPDSAGERRRSGGGVRTQEGVESEHDAPQAGRRQYSAEEDLEEDRGVKLGLGDFIFYSVLVGKAAATGGDWNTTLACFVAILIGLCLTLLLLAIFKKALPALPISITFGLVFYFSTDNLVRPFMDSLAAHQYYI
Protein: Glycerol-3-phosphate dehydrogenase (EC 1.1.5.3) (Q384S7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Glycerol-3-phosphate dehydrogenase [NAD
- Dihydroxyacetone phosphate acyltransferase, putative
- Glycerol-3-phosphate dehydrogenase
- Glycerol-3-phosphate acyltransferase, putative
- glycerol kinase
- glycerol kinase
- glycerol kinase
- glycerol kinase
- Phosphatidic acid phosphatase, putative
- Phosphatidic acid phosphatase protein, putative
Sequence:
MSRIPEKILCASAGAFVGCIGFSYTNPKWTQRRFNPKNVPPLLYQQTPSREDCLKRMEAFNSPENPMDVIIVGGGSVGAGVALDATTRGMTVGLFEMNDYASGTSSRSTKLIHGGIRYLEKAVFKLDMQQLMLVAEALRERIIMSHQAPHLCRSIPTMIPCYNPIDIAKFWCGVKLYDIIAMWERGTLEYAGYLTPYAALKKFPYLKNGTNNGKILLGAVEYYDGQMNDARLCLSAALTAASYGAATVNYAKVEKMEVVQNKMGEQVVKATVQDRINSNTLTVYGKSVVNAGGPFTARIQKLITDKTSVRMAPSSGTHIIIDRKYCPRDSAMVIPSNDGRVVFSAEWLGGCLVGTTDKGCEVTEDIRPTKSDIKFLLNNVEPYVGKVSEKDVLSAWCGIRPLALPENAEGSDTQNIVREHMVVVDKDNLMVSVVGGKWTTYRKIAQDTVDALYSSLLKGRVECKPCITEELQVIGAHELETVPEEPKISISNKVHKFWRRQYGDRYHVLADMVREDPSLLKPLHPEEPVLAADVVYSAQREHCERVVDFISRRTRLSFLNVEHAKAIIPEVAQIMATTKNWSRARKSEEVAHALAALESFHGQ
Protein: Radiation-sensitive protein 28 (Q12021)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in transcription-coupled repair nucleotide excision repair (NER) of UV-induced DNA lesions.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- DNA repair and recombination protein RAD26
- DNA repair protein RAD7
- DNA repair protein RAD16
- UV excision repair protein RAD23
- General transcription and DNA repair factor IIH subunit SSL1
- DNA repair protein RAD4
- DNA repair protein RAD14
- DNA repair protein RAD34
- RNA polymerase II transcription factor B subunit 3
- DNA-directed RNA polymerase II subunit RPB4
Sequence:
MDPFLEFRVGNISLNEFYRRTIQSEFERILEDPLSNMKNYRFSKQSNYSTKEKTPLSIGVNCLDIDDTGQVLLGGGDDGSLSIWGLDESLHRNDEGEQELINKRLNYIKRQPHQSDDEPAQIMGYKNKRTRINDNNTMRLVHSFQTQRNKYRMYRQSSAAVPVQRSHISNKTDSPIGFSETLSETDSEASISHHKYGITTLKWYKADNGMFFTGSNDKTVKIWDTNRFEAVQDINLGYKINQIDNNVVDDSSLLVVASEDYYPRLIDLRTMNSGVTALGMGNQTRMQSEILCCKFNPVREQIIACGDMEGGVKLWDLRMRNRLYSELKRNKNRFKTINNDDNDDQSDVYFSSNQSKAHLRCCSDIVWNSEGSELCSVGMDGKLNVWRPFTEILQPEGLASYSQLGTQDLSRIKYKKRVSRRLLWFDKFLLCITDNGEVEIYNTEEKKLWNKLEYPMVNQVKKNQASHCQFSSMIVQTNIMNSVGLKLFFGTNNNTVSDGGSIFECS
Protein: Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial (EC 2.3.1.12) (70 kDa mitochondrial autoantigen of primary biliary cirrhosis) (PBC) (Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex) (M2 antigen complex 70 kDa subunit) (Pyruvate dehydrogenase complex component E2) (PDC-E2) (PDCE2) (P10515)
Organism: Homo sapiens (Human)
Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P08461}.
Interaction partners:
- Dihydrolipoyl dehydrogenase, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Pyruvate dehydrogenase protein X component, mitochondrial
- [Pyruvate dehydrogenase
- Citrate synthase, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
- 2-oxoglutarate dehydrogenase complex component E1
- ATP-citrate synthase
Sequence:
MWRVCARRAQNVAPWAGLEARWTALQEVPGTPRVTSRSGPAPARRNSVTTGYGGVRALCGWTPSSGATPRNRLLLQLLGSPGRRYYSLPPHQKVPLPSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRDVPIGAIICITVGKPEDIEAFKNYTLDSSAAPTPQAAPAPTPAATASPPTPSAQAPGSSYPPHMQVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLCIIVEKEADISAFADYRPTEVTDLKPQVPPPTPPPVAAVPPTPQPLAPTPSAPCPATPAGPKGRVFVSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSFVPSKVAPAPAAVVPPTGPGMAPVPTGVFTDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGEVLLVRKELNKILEGRSKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKLVPADNEKGFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL
Protein: Protein CANDIDATE G-PROTEIN COUPLED RECEPTOR 7 (AtCand7) (F4JY11)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a role in plants and microbes interactions. G-protein coupled receptor involved in root growth mediated by the bacterial quorum-sensing signals N-acyl-homoserine lactones (AHLs).
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein CANDIDATE G-PROTEIN COUPLED RECEPTOR 8
- Protein CANDIDATE G-PROTEIN COUPLED RECEPTOR 2
- RING-type E3 ubiquitin transferase
- AT3g59090/F17J16_140
- Transmembrane 9 superfamily member 12
- Probable methyltransferase PMT26
- Lung seven transmembrane receptor family protein
- Heptahelical transmembrane protein 5
- Heptahelical transmembrane protein 2
- MLO-like protein 9
Sequence:
MAKMPLSVVVFLLFSAAFLAVSMAEIKSLVISDDARPMILFEKFGFTHTGHVTVSISSVSVVSTSSDPNPEASRLGFFLLSEESLLQVLLEIQQNPRFCVLDSHYVTHLFTFRDLSPPPNSRFNQSYPVTSPNEYSLFFANCVPETKVSMAVRTEMYNKDPNGSKDYLPAGSTQLPTLYSFFFLCYVAFLGFWSYTCWTNKQTVHRIHLLMAGLLLIKSLNLICAAEDKHYVKITGTPHGWDILFYIFQFIRVVLLFTVIILIGTGWSFLKPFLQEKEKNVLIIVIPLQVLANIASIVIGETGPFIKDWVTWNQVFLLVDIICCCAIIFPIVWSIRSLRETSKTDGKAARNLSKLTLFRQFYIVVIGYLYFTRIVVFALKTIAAYKYQWVSFAAEEIVSLVFYVIMFHMFRPEEKNEYFAVDDDEEEAAALALRDEEFEL
Protein: Homoaconitase, mitochondrial (EC 4.2.1.36) (Homoaconitate hydratase) (Q9UT74)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the reversible hydration of cis-homoaconitate to (2R,3S)-homoisocitrate, a step in the alpha-aminoadipate pathway for lysine biosynthesis.
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- Homoisocitrate dehydrogenase
- 3-isopropylmalate dehydrogenase
- Multifunctional tryptophan biosynthesis protein
- Saccharopine dehydrogenase [NADP
- Adenylosuccinate synthetase
- Dihydroorotate dehydrogenase
- Histidinol-phosphate aminotransferase
- Probable citrate synthase, mitochondrial
- Probable isocitrate dehydrogenase, mitochondrial
- Saccharopine dehydrogenase [NAD
Sequence:
MDSGEMHHPYQAFSKVGKCEISQTNPSFSSGMRCLVRSADIQFKGICGLTRGFASFNKPPQTITEKIVQKFAQNIPENKYVRSGDYVTIKPKHCMSHDNSWPVALKFMGIGAKKVFDNRQIVCTLDHDVQNKSEANLRKYKNIESFAKGQGIDFYPAGRGIGHQIMVEQGYAMPGSMAVASDSHSNTYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPIARVNLVGQLPKGLSGKDIIVSLCGAFNHDEVLNHAIEFYGEGLNSLSIESRLTIANMTTEWGALSGLFPTDEKLLAWYEDRLKFLGPNHPRVNRETLDAIKASPILADEGAFYAKHLILDLSTLSPAVSGPNSVKVYNSAATLEKKDILIKKAYLVSCTNGRLSDIHDAAETVKGKKVADGVEFYVGAASSEVEAAAQKNGDWQTLIDSGARTLPAGCGPCIGLGTGLLKDGEVGISATNRNFKGRMGSREALAYLASPAVVAASAIAGKIVAPEGFKNAVSLVSAVDITDKVNKQTASKSSTEAVDSETAIIDGFPSIVAGEIVFCDADNLNTDGIYPGRYTYRDDITKEEMAKVCMENYDSEFGKKTKKDDILVSGFNFGTGSSREQAATAILSRGIPLVVGGSFSDIFKRNSINNALLAIQLPDLVQKLRTAFANESKELTRRTGWHLKWDVRKSTVTVTTSDNKEMSWKIGELGNSVQSLFVRGGLEGWVKHEISKSN
Protein: Phosphotransferase (EC 2.7.1.-) (Q95PL2)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MSRRLNNILEHISIQGNDGETVRAVKRDVAMAALTNQFTMSVESMRQIMTYLLYEMVEGLEGRESTVRMLPSYVYKADPKRATGVFYALDLGGTNFRVLRVACKEGAVVDSSTSAFKIPKYALEGNATDLFDFIASNVKKTMETRAPEDLNRTVPLGFTFSFPVEQTKVNRGVLIRWTKGFSTKGVQGNDVIALLQAAFGRVSLKVNVVALCNDTVGTLISHYFKDPEVQVGVIIGTGSNACYFETASAVTKDPAVAARGSALTPINMESGNFDSKYRFVLPTTKFDLDIDDASLNKGQQALEKMISGMYLGEIARRVIVHLSSINCLPAALQTALGNRGSFESRFAGMISADRMPGLQFTRSTIQKVCGVDVQSIEDLRIIRDVCRLVRGRAAQLSASFCCAPLVKTQTQGRATIAIDGSVFEKIPSFRRVLQDNINRILGPECDVRAVLAKDGSGIGAAFISAMVVNDK
Protein: DCC family protein At1g52590, chloroplastic (Q9SSR1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
- Acyl-CoA N-acyltransferases
- N-alpha-acetyltransferase MAK3
- Small nuclear ribonucleoprotein-associated protein
- Small nuclear ribonucleoprotein-associated protein
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein E
Sequence:
MAILIPASFGRLTITSRAQVRVRVSASANQRTIRRDSVDWVKETSSFFEEDKRPIMLFDGVCNLCNGGVKFVRDHDRNRSIRFEALQSEAGKKLLLRSGRAPDDISSVVLVENDRSYIKSEAVLKIMKYIDLPFPQLAFFLQFAPLFVRDFLYENVANNRYAMFGRSDSCEL
Protein: Ras-related protein Rab-1D (Q54NU2)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
Sequence:
MSMAPEHDFFFKILLIGDSGVGKSCLLLRFADDSWTDTHISTIGVDFKIKTLNLDGKTIKLQIWDTAGQERFRTITSSYYRGAQGIILVYDCTDQDSFTNVKQWMGEIDRYACENVNKLLVGNKTDLVNEKVVDSNQAKSFAESYGIPFIETSAKNATNVEECFISMARDIKNRLADIQETPKPDEVDIKSKNKTKSGGKKSFC
Protein: Succinate dehydrogenase assembly factor 4, mitochondrial (Q6FQ39)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
Sequence:
MLRHNRHLFSAVARSSVLISRPVAIRCINTERIPSPPKLPREEQEEFERLQRIAHSQEAIDEYNRKIKGDHTKESLNNEMLTKNDIGSFSPEFSKTIPEFEGDVNPKTGEIGGPKQDPLKHGDYSFNGRVTDF
Protein: Calcium-transporting ATPase (EC 7.2.2.10) (A0A1D8PQK6)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}. Membrane {ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361146}.
Interaction partners:
- Calcium-transporting ATPase
- GDT1 family protein
- Vacuolar calcium ion transporter
- Calcium-channel protein CCH1
- Rcn1p
Sequence:
MSANPYDIEHKLPPQRANTPSLKYSQKSIEETAADLQTDIKLGLTNSQDVLNRRSIHGINELNGDEEESLLWKFISSFYQDPLILLLIGSAVISFWMGNKDDAISITLAITIVVTVGFVQEYRSEKSLEALNKLVPAEAKLTRTGSTSSVLAQVLVPGDLVHFSQGDRIPADIRLTEAVHLTIDESNLTGENRPVKKTVDTVNSSDPAVTERTDIAFMGTLVRDGHGSGIVVATAGQTVFGSVFEMMSDIEKPKTPLQQAMDKLGKDLSIFSFIVIGIICLIGIFQGRSWLDMFQISVSLAVAAIPEGLPIIVTVTLALGVLRMARQKAIVRRLPSVETLGSVNVICSDKTGTLTQNHMTVTKIWTADFKGSFNTPFLAVERLDDNTLHHQLTSNMHKVLECGNICNNARYSTESEKYVGNPSDIALVECLPHFGLEDMRGQKQRLYELPFSSNRKYMAVCVHTGDIEKSETIAKGATEKILQLCDRYYDENGSVKPLTEAIEESIHEKSRSLARDGLRVLAFAKNNKKFDEKTTEPTDLVFCGLIGMKDPPRPKVGQSIARLMQGGVHVIMITGDSPTTAVNIARQIGIPVVGDHAVLTGDQIDSLSEEALTKAIHDVSVFARTTPEHKVTIVKALQRRGDIVAMTGDGVNDAPALKLADIGIAMGKNGTDVAKEAADMVLTDDDFSTILSAIEEGKGIFNNIQNFITFQLSTSIAALTLVALSTFFGLPNPLNAMQILWINILMDGPPAQSLGVEPVDHEVMNKPPRKRNDVILTQQVIKRVLQSAAIIIVGTMYVFIKEMTDGVITARDTTMTFTCFVLFDMFNALSCRHYSKSIFELGMTNQMFNFAVLGSLIGQFCAVYVPFFQSIFQTEALNFGDILRLVILTSTVFAVDEIRKWLRRRKTVYTNNYSYGV
Protein: Collagen type IV alpha 2 (O18407)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302}.
Interaction partners:
Sequence:
MLPRDLRHLSGLPGVVYLLGSLVSVTLADGKICNTTLCDCKGIKGRMGAPGPIGVPGLEGPAGDIGPPGRAGPLGEKGDVGEYGEQGEKGHRGDIGPKGEMGYPGIMGKSGEPGTPGPRGIDGCDGRPGMQGPSGRPGQNGVRGPPGKSRQQGPPGEAGEGGINSKGTKGNRGETGQPGGVGPPGFDGDRGSKGDTGYAGLTGEKGDPGLPGPKGDTGAVSELPYSLIGPPGAKGEPGDSLSGVLKPDDTLKGYKGYVGLQGDEGPQGPTGEQGAVGRNGLPGARGEIGGPGERGKPGKDGEPGRFGDKGMKGAPGWTGADGLDGSPGERGEDGFTGMPGVQGGAGPPGIYDPSLTKSLPGPIGSQGDIGPPGEQGPPGLPGKPGRRGPIGLAGQSGDPGLNGSRGPPGRSERGEAGDYGFIGPPGPQGPPGEAGLPGRYGLHGEPGQNVVGPKGEPGLNGQPGLEGYRGDRGEVGLPGDKGLPGEGYNIVGPPGSQGPPGFRGLPGDDGYYGLRGLPGEKGLRGDDCPVCNAGPRGPRGQEGDTGYPGSHGNRGAIGLAGPRGVQGLQGNPGRAGHKGLPGPAGIPGEPGKVGAAGPDGKAIEVGSLRKGEIGDTGDSGHRGDTGDDGEKGRDGSDGSKGERGETGQRGDYGDAGYQGRDGEPGRDGRDGAPGRNATTPKVYLIGEPGYDGIKGERGDDGDTGFKGVKGEPNPGQIYDNTGEPGEDGYTGPKGVKGAKGEQGAIGLRGEIGDRGPAGEVIPGPVGAKGYPGPTGDYGQQGAPGLPGRDGEPGLDGGIGYKGQRGVPGQEVIQGEIGPPGRSGIKGFPGDVGAPGQYGLAGRPGPKGVKGEQGPDGAVGQTGLPGNKGQRGDFLVGPPGPKGQPGRNGRQAPHGAKGQKGEVGSLGQNGQNGAKGSIGFSGRRGLLGNLQGLPGSPGIPGLPGMIGEIGERGEIGYNGRQGDIGPRGPNGEFGPKGLSGDDGPDGYPGANGLPGRKGETGNPGFPGRPGAKGVAAYSGIKGDDGESGLTGPIGYPGAPGVKGQRGPVGDSQPALDGVAGRKGEVGSPGPNGLPGRHGLKGQRGDRGLPGQQGRPGEPGAKGLGGYPGRNGINGLKAATGFPGPQGPKGPQGESGVVGLDGRNGQIGDQGPRGLIGEQGEQGEQGDEGEVGIPGRLENLRDRSFYRGFTGDQGLQGERGEQGDMGPIGFIGPPGAKGERGDIGYAGQLGFDGAEGLKGFQGDQGPRGPPGITLPAEKGDEGVAGLDGRAGRPGHFGQKGAPGPPGENGPNGAIGHRGPQIQGPPGPQGDVGFPGAPGHNGRHGLIGPKGELGDMGRQGERGESGYAIVGRQGDIGDIGFQGEPGWDGAKGEQGYPGLPGKNGRVGAPGPRGPTGDAGWGGIDGMDGLVGPKGQPGVTYSYSMARPGDRGEPGLDGFQGEEGDGGAPGLIGFQGQRGAVGYRGDQGEVGYTGADGPQGQRGDKGYMGLTGAPGLRGLPGPQGEPAPAPPAPKSRGFIFARHSQSVHVPQCPANTNLLWEGYSLSGNVAASRAVGQDLGQSGSCMMRFTTMPYMLCDITNVCHFAQNNDDSLWLSTAEPMPMTMTPIQGRDLMKYISRCVVCETTTRIIALHSQSMSIPDCPGGWEEMWTGYSYFMSTLDNVGGVGQNLVSPGSCLEEFRAQPVIECHGHGRCNYYDALASFWLTVIEEQDQFVQPRQQTLKADFTSKISRCTVCRRRGNSFVARTAKSRADASSGVHRWFCLE
Protein: 2-hydroxyacyl-CoA lyase 1 (EC 4.1.2.63) (2-hydroxyphytanoyl-CoA lyase) (2-HPCL) (Phytanoyl-CoA 2-hydroxylase 2) (Q9QXE0)
Organism: Mus musculus (Mouse)
Function: Peroxisomal 2-OH acyl-CoA lyase involved in the cleavage (C1 removal) reaction in the fatty acid alpha-oxydation in a thiamine pyrophosphate (TPP)-dependent manner (By similarity). Involved in the degradation of 3-methyl-branched fatty acids like phytanic acid and the shortening of 2-hydroxy long-chain fatty acids (By similarity). Plays a significant role in the biosynthesis of heptadecanal in the liver.
Subcellular location: Peroxisome {ECO:0000250|UniProtKB:Q9UJ83}.
Interaction partners:
- Peroxisomal targeting signal 1 receptor
- PEX5-related protein
- Acetylcholinesterase collagenic tail peptide
Sequence:
MPESNSAEGSDRSEEQVSGAKVIAQALKTQDVEYMFGVVGIPVTEIALAAQELGIKYIGMRNEQAACYAASAVGYLTGRPGVCLVVSGPGLIHALGGMANANMNCWPLIVIGGSSERNQEAMGAFQEFPQVEACRLYTKFSARPSTIELIPFIIEKAVRSSIYGRPGACYIDIPADFVTLQANVTSIKYKECCMPPPVSMAETSAVCAAASVLRDAKQPLLIIGKGAAYSHAEDSIRKLVEQCSLPFLPTPMGKGVVPDNHPNCVGAARSRALQSADVIVLFGARLNWILHFGLPPRYQADVKFIQIDICAEELGNNVRPSVILLGDIDAVSKQLLEQFDKTPWQCPPDSQWWKTLREKMKSNEAISKELASQKSLPMNYYTVFYHVQEQLPRDSFIVSEGANTMDIGRTMLQNCLPRHRLDAGSFGTMGVGLGFAIAAALVAKDRSPGQRVICVEGDSAFGFSGMEVETICRYNLPIILLVVNNNGIYQGFDADTWEKMLHFQEAATTVPPMCLLPNSHYEQVMTAFGGKGYFVRTPEELQHSLRQALQDTSKPCLLNIMIEPQSTRKAQDFHWLTRSNM