wanglab/gogpt-training-data huggingface dataset:
Protein: Protease 3 (EC 3.4.24.55) (Pitrilysin) (Protease III) (Protease pi) (P05458)
Organism: Escherichia coli (strain K12)
Function: Endopeptidase that degrades small peptides of less than 7 kDa, such as glucagon and insulin.
Subcellular location: Periplasm.
Interaction partners:
- RecBCD enzyme subunit RecB
- RecBCD enzyme subunit RecD
- RecBCD enzyme subunit RecC
- Protease 2
- Periplasmic serine endoprotease DegP
Sequence:
MPRSTWFKALLLLVALWAPLSQAETGWQPIQETIRKSDKDNRQYQAIRLDNGMVVLLVSDPQAVKSLSALVVPVGSLEDPEAYQGLAHYLEHMSLMGSKKYPQADSLAEYLKMHGGSHNASTAPYRTAFYLEVENDALPGAVDRLADAIAEPLLDKKYAERERNAVNAELTMARTRDGMRMAQVSAETINPAHPGSKFSGGNLETLSDKPGNPVQQALKDFHEKYYSANLMKAVIYSNKPLPELAKMAADTFGRVPNKESKKPEITVPVVTDAQKGIIIHYVPALPRKVLRVEFRIDNNSAKFRSKTDELITYLIGNRSPGTLSDWLQKQGLVEGISANSDPIVNGNSGVLAISASLTDKGLANRDQVVAAIFSYLNLLREKGIDKQYFDELANVLDIDFRYPSITRDMDYVEWLADTMIRVPVEHTLDAVNIADRYDAKAVKERLAMMTPQNARIWYISPKEPHNKTAYFVDAPYQVDKISAQTFADWQKKAADIALSLPELNPYIPDDFSLIKSEKKYDHPELIVDESNLRVVYAPSRYFASEPKADVSLILRNPKAMDSARNQVMFALNDYLAGLALDQLSNQASVGGISFSTNANNGLMVNANGYTQRLPQLFQALLEGYFSYTATEDQLEQAKSWYNQMMDSAEKGKAFEQAIMPAQMLSQVPYFSRDERRKILPSITLKEVLAYRDALKSGARPEFMVIGNMTEAQATTLARDVQKQLGADGSEWCRNKDVVVDKKQSVIFEKAGNSTDSALAAVFVPTGYDEYTSSAYSSLLGQIVQPWFYNQLRTEEQLGYAVFAFPMSVGRQWGMGFLLQSNDKQPSFLWERYKAFFPTAEAKLRAMKPDEFAQIQQAVITQMLQAPQTLGEEASKLSKDFDRGNMRFDSRDKIVAQIKLLTPQKLADFFHQAVVEPQGMAILSQISGSQNGKAEYVHPEGWKVWENVSALQQTMPLMSEKNE
Protein: Chaperonin GroEL (EC 5.6.1.7) (60 kDa chaperonin) (Chaperonin-60) (Cpn60) (Q9KJ23)
Organism: Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533)
Function: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00600}.
Interaction partners:
Sequence:
MAKEIKFSENARHSLLKGVDKLADTVKTTLGPKGRNVVLEKSYGAPDITNDGVTIAKSIELENHFENMGAKLVSEAAQKTNDIAGDGTTTATVLTQAIVREGMKNVTAGANPVGIRRGIETATKAAVDELHKISHKVSTKDEIAQVASVSSASTEVGNLIADAMEKVGHDGVITIEESKGIDTELSVVEGMQFDRGYLSQYMVTDNDKMEADLDNPYILITDKKISNIQDILPLLQEIVQQGKSLLIIADDVDGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAMLEDIAILTGGTVISSDLGLELKDTKIDQLGKAGKVTVTKDSTTIVEGAGSKEAIAERVDQIKKQIADTTSDFDREKLQERLAKLAGGVAVIKVGAATETELKERKYRIEDALNATRAAVEEGYVAGGGTALVDVMKSIQGTVKGDSEDAETGVKIVMKALGAPVRQIAENAGKDGAVILDHLEHEDPEVGYNAATNKWENMVKAGIIDPTKVTRSALQNAASIAALLLTTEAVVADAPEDDKNQAPAAPNPGMGMGM
Protein: Cytochrome c oxidase subunit 5A, mitochondrial (Cytochrome c oxidase polypeptide Va) (P11240)
Organism: Rattus norvegicus (Rat)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P00426}; Peripheral membrane protein {ECO:0000250|UniProtKB:P00426}; Matrix side {ECO:0000250|UniProtKB:P00426}.
Interaction partners:
- Cytochrome c oxidase subunit 3
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome c oxidase subunit 2
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Cytochrome c oxidase subunit 6C-2
- Cytochrome c oxidase subunit 6A1, mitochondrial
- Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
- Cytochrome c oxidase subunit 5B, mitochondrial
Sequence:
MLAAALRRCTAAAAARGLLHPVSAPSPAAAVCSIRCYSHGSHETDEEFDARWVTYFNKPDIDAWELRKGMNTLVGYDLVPEPKIIDAALRACRRLNDFASAVRILEVVKDKAGPHKEIYPYVIQELRPTLNELGISTPEELGLDKV
Protein: Leucine-rich repeat (LRR) family protein (Q9FHI4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSTKECDIYKIINILSQLDSDLKKIPVSDKVISHKEQQGEPSEEKRSWWVRVRGSLKRIGKAKKEAFNNASDSGGSQGGSRRSVQNIEEDQKNEDLEIRKLQNDIRQMIAAFKNLTQFQTDMSKNLERDLRSTKLIAILQKKNSFGSRSHVVKEIRRKVSALKCQIPSLLHKQSSRKISITDSQTAEENDEISETGIDIYLPGLHFSEKFKTSSAFEEVVEKFQGLDDFTQKLCLLSFAVFPENREVKRTMLMYWWIGEGFISCDDSENLVTRILDSFSDKKLLEPVEDERKLLPSSYKMEPHVHSAVIYLAKEMDLFELYNKNGKLIMKKSSKKKVCLVKGSSLLRDAKTSVMEPKTLQTVFNSSERYPDFTFKWFPLMDSLRVLYLGRWEQTAKRHIEVESTEFLKNMKSLKNLRLASFQGISRIERLENSICALPELVILDLKACYNLEVLPSDIGLFEKLIYLDVSECYMLDRMPKGIAKLSRLQVLKGFVISESDHENNCAVKHLVNLRKLSITVNKYSFKVESLMESLTGLQGLESLKIAWGACEEPNEAVESRETTNEKKENQGGLATDKKLKDLMEREDDQVQNYGQTSKEEKGNVEETGKQEDGDQGDGINEEANLEDGKKHDEGKEERSLKSDEVVEEEKKTSPSEEATEKFQNKPGDQKGKSNVEGDGDKGKADLEEEKKQDEVEAEKSKSDEIVEGEKKPDDKSKVEKKGDGDKENADLDEGKKRDEVEAKKSESGKVVEGDGKESPPQESIDTIQNMTDDQTKVEKEGDRDKGKVDPEEGKKHDEVEGGIWKSDNGVEGVDKASPSRESTDAIENKPDDHQRGDKQEEKGDGEKEKVNLEEWKKHDEIKEESSKQDNVTGGDVKKSPPKESKDTMESKRDDQKENSKVQEKGDVDKGKAADLDEGKKENDVKAESSKSDKVIEGDEEKNPPQKSKDIIQSKPDDHREISKVQEKVDGEKNGDDLKKLDGGGEAKTQKSRKTTKFGKNVSDHPKRDNTMAEDIHETQSPSRKSKSSKAKWLTGRGNQTKKWGIGWQEDPVVDDTYTLPSNLKKLELECFPETKPPSWLNPKDLKNLKKLSIKGGKLSRIGDESRITEDKWDVEILRLKYLHEFKVEWRDLQTLFPKMTLLEKYKCPKIAFCPTDGNGVWTSSPNM
Protein: Uncharacterized protein YbjN (P0AAY6)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Ribosomal protein bS6--L-glutamate ligase
- Oxygen-insensitive NADPH nitroreductase
- Uncharacterized protein YbjC
Sequence:
MTSLVVPGLDTLRQWLDDLGMSFFECDNCQALHLPHMQNFDGVFDAKIDLIDNTILFSAMAEVRPSAVLPLAADLSAINASSLTVKAFLDMQDDNLPKLVVCQSLSVMQGVTYEQFAWFVRQSEEQISMVILEANAHQLLLPTDDEGQNNVTENYFLH
Protein: Serine palmitoyltransferase 2 (SPT 2) (EC 2.3.1.50) (Long chain base biosynthesis protein 2) (Q09925)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalytic subunit of serine palmitoyltransferase (SPT), which catalyzes the committed step in the synthesis of sphingolipids, the condensation of serine with palmitoyl CoA to form the long chain base 3-ketosphinganine.
Subcellular location: Cytoplasm {ECO:0000250}. Endoplasmic reticulum {ECO:0000269|PubMed:16823372}. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Serine palmitoyltransferase 1
- PIGF/3-ketodihydrosphingosine reductase fusion protein
- Uncharacterized protein C119.09c
- Sphingolipid delta
- Serine/threonine-protein kinase tor1
- Serine/threonine-protein kinase tor2
- Tryptophan synthase
- Target of rapamycin complex 1 subunit mip1
- Target of rapamycin complex subunit wat1
- Serine racemase
Sequence:
MAQADFVSPTSIDVSEKKEVEFHKKVDHVENPPLSTESAKLEAEEVAAEKLNSEHLLENEFAPITDPTHRRVSKNPDGAELFQFEDEPSYYYVVATYLTYLVLIIIGHVRDFFGKRFHKDDYKYLKDNDGYAPLYNHFDNFYVRRLQHRINDCFSRPTMGVPGRVIRLMNRYSTDSNSTFKLTGDTSLALNVSSYNYLGFAQSHGPCATKVEEAMQKYGLSTCSSNAICGTYGLHKEVEELTANFVGKPAALVFSQGFSTNATVFSTLMCPGSLIISDELNHTSIRFGARLSGANIRVYKHNDMTDLERVLREVISQGQPRTHRPYSKILVVIEGLYSMEGNFCDLPKVVELKNRYKFYLFIDEAHSIGAIGPRGGGICDYFGISTDHVDILMGTFTKSFGAAGGYISATPNIINKLRVTNPGYVYAESMSPAVLAQIKSSFLEIMDNSPTSAGLERIERLAFNSRYIRLGLKRLGFIIFGNDDSPVVPLLLYNPGKINAFSHEMLKRGIAVVVVGYPACPLLTSRVRFCFSASHNKADMDYFLRACDEVGEKLQLKFSTGAAGEDVGKTNVEKMKKNQGWFKPPRWKIEDVLKHGVHDALTQ
Protein: N-cym protein (N-myc opposite strand) (P40205)
Organism: Homo sapiens (Human)
Function: Regulates stability of MYCN in neuroblastoma cells by inhibiting GSK3B-mediated MYCN phosphorylation. Inhibits GSK3B activity by promoting its phosphorylation at 'Ser-9'.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24391509}. Nucleus {ECO:0000269|PubMed:24391509}.
Interaction partners:
Sequence:
MQHPPCEPGNCLSLKEKKITEGSGGVCWGGETDASNPAPALTACCAAEREANVEQGLAGRLLLCNYERRVVRRCKIAGRGRAPLGTRPLDVSSFKLKEEGRPPCLKINK
Protein: Protein borderless (Q9U4G1)
Organism: Drosophila melanogaster (Fruit fly)
Function: In the developing eye, has a role in axonal targeting of the R7 photoreceptor where it functions together with tutl. Probably mediates homotypic cell adhesion; the effect is inhibited by Lar.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}. Cell projection, axon {ECO:0000269|PubMed:24174674}.
Interaction partners:
Sequence:
MPAKRSRTFRQSGSALLALLAIILLMNISCTSAARDHRRQTNLEAKVGSHVVFNCYIDFPFDAPIPYLVHWTKDNKKIFTWYEQETSTSELFNGRLHLVENHPEFGRASVNLTAIRESDQGWYHCQVSFPNRSPSVRNNGTAYHLAVQGGSLIRIPPVNQTIREGQTAFFHCVMKHPENSQASWYKDGVLLQEVQDLVRRFYMGPDGSLSIDPTMMSDLGEYECKVRNSDGELQTAKAFLNIQYKAKVIYAPPEVFLPYGQPAVLDCHFRANPPLKNLRWEKDGLLFDSYNVPGVFYKMNGSLFFAKVDENHAGSYTCTPYNDLGTDGPSPVISVIVLRPPIFSVTPKAIYIQKLGEAAELPCEAIDRDGNNRPSIIWGRKDGQPLPADRFSLSGGNLTITGLVEGDRGIYECSATNEAATITAEAELMIENIAPRAPYNLTANSTETCITIRWQPGYLRPNLEYTVWYRLMEAPEWRTLRVLDKKVMEATVQHLQPGKEYEFMVLSQDKYGDGMFSKQFRFQTLPSPIRADDFDAQQLQHDLGQVTAPAGGLGAPWNLTAISNQQGWLLHWEHPVQGLEGLRLYAVRWWKEPEHFLIGHAETFDNYYQLRHLKEDTLFKVQVLAVGTETQQSVPSHELLIDVPSQRKVRALIIGSSVGVIFLLCALCAFLYVKRSCLRHLFAKDSSASEDEDTAESGDCDSDEQDQRDRDSIKIRQST
Protein: TNF receptor-associated factor homolog 1a (MATH domain-containing protein At5g43560) (Protein MUTANT SNC1-ENHANCING 14) (Q8RY18)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions redundantly with TRAF1B in the regulation of plant immune response. Contributes to the turnover of the nucleotide-binding domain and leucine-rich repeat-containing (NB-LRR) immune receptors SNC1 and RPS2. May associate with an E3 ubiquitin-protein ligase complex, which modulates ubiquitination and subsequent degradation of NB-LRR immune sensors to maintain their homeostasis. Functions redundantly with TRAF1B in the regulation of autophagosome formation. Required for SINAT1- and SINAT2-mediated ubiquitination and destabilization of ATG6. Functions as molecular adapter that helps to regulate autophagy by modulating ATG6 stability.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:28351989}. Note=Predominantly expressed in the cytoplasm. Associates with starvation-induced autophagosomes in continuous darkness. {ECO:0000269|PubMed:28351989}.
Interaction partners:
- Putative E3 ubiquitin-protein ligase SINAT1
- E3 ubiquitin-protein ligase SINAT2
- Probable inactive E3 ubiquitin-protein ligase SINAT6
- Beclin-1-like protein
- Autophagy-related protein 13b
- Autophagy-related protein 13a
- Cytochrome c-type biogenesis protein CcmE homolog, mitochondrial
- Actin cross-linking protein, putative
- Serine/threonine-protein kinase ATG1b
- Transcription initiation factor TFIID subunit 15b
Sequence:
MSESTNEDSGAGRSSLEENSNGQRSQSEEAIAEWRSSEQVENGTPSTSPPYWDIDDDDDFGSKPSQLFGKNTWTIEKFSDINKRELRGDVFEVGGYKWYILIYPQGCDVCNHLSLFLCVAHHEKLLPGWSHFAQFTIAVSNKDPKKSKHSDTLHRFWKKEHDWGWKKFIELPKLKEGFIDDSGCLTIKAQVQVIRERVDRPFRCLHYKYREELVRVYLGNVEQICWRFVEEKRSKLGRLIEDKAKWKSFCAFWMGLDQNSRRRMSREKMDVILKIVVKHFFVEKEVTSTLVMDSLYSGLKALEGQNKNKESRPRLMDTEESTAPIVSVDKDSFALVDDVLLLLEKAALEPLPKKEEKSSQNRTKDGNAGEEFSREAVERDDRRLTELGRRTVEIFVLAHIFSNKIEVAYQEAIAWKRQEELIREEEEAWLAESEQKGKRGASEKEKKSKKKQAKQKKNKNKGKEMRKEDKVRTQTEEREIEKEECVRAIAESSAEKPDTLGDVSDVSDSVDSSAEILQLDSEDRESSPVHWEMDASEVHPPSAGDTSRGRGNSFSIPNGVAERKGLSTMDDSSSTCSNDSIQSGVANGSYKGNVLNCQSQKWFSNGKIQPGKVSDSNSLASEKEHQPSRLASDPKNQSHSSDIRRVGEADIVISHIQKPESPKERSPVSKDPNMIQMKEKSAAVLSPSRAAPWNPPSPVQAKPEKKGVSNVEAVPNRKVISVKSPSSHHASPSREAQLQTVGPRADIQKIASPKPVEQPAPPMSRPLSAPIIPPTQAAPVISAVQTSTASLARSMSSTGRLGSPTHSQAYNPQSYKHAIVGSSGFTHPSSQSSGTSTLPPYSHPSPISVSNQSGFPINVGSWDVSSGGLLWTGGSSSTRDTTTTISGNHKTNTYNAPVVTTSIRPTNVQIGRTAQSLMTDEFPHLDIINDLLADEHGTMDNSVYRVPQQFNNQYSYHGGADLGISSRSRSYSDDGFHQSYGEYMPHSASSSPYGNGQTQSQWQMANMDFSLPAMRNQDDVSASATATYSYFDLDSSNPNLSGINGYRDFRPSNGH
Protein: Receptor expression enhancing protein A, isoform L (A8DYN0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MHRTQDELDDVMMSSMTSSAVVMRSTATGARLLRPRNQTPVGRSGSGTRHSTGMYFTEVDVTAKNAGDFNYNIRSQDDISSGYSSAEPVSGLSRTSSMTNASKARAKSKRNEDKSMSASCTTLPRSSSRKSERSQGGTATGQMKTRNKSEK
Protein: Actinin alpha 4 isoform 1 (A0A0S2Z3G9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVDYHAANQSYQYGPSSAGNGAGGGGSMGDYMAQEDDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIDEDFRDGLKLMLLLEVISGERLPKPERGKMRVHKINNVNKALDFIASKGVKLVSIGAEEIVDGNAKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKMLDAEDIVNTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEHLMEDYEKLASDLLEWIRRTIPWLEDRVPQKTIQEMQQKLEDFRDYRRVHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGKMVSDINNGWQHLEQAEKGYEEWLLNEIRRLERLDHLAEKFRQKASIHEAWTDGKEAMLKHRDYETATLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSHNVNTRCQKICDQWDALGSLTHSRREALEKTEKQLEAIDQLHLEYAKRAAPFNNWMESAMEDLQDMFIVHTIEEIEGLISAHDQFKSTLPDADREREAILAIHKEAQRIAESNHIKLSGSNPYTTVTPQIINSKWEKVQQLVPKRDHALLEEQSKQQSNEHLRRQFASQANVVGPWIQTKMEEIGRISIEMNGTLEDQLSHLKQYERSIVDYKPNLDLLEQQHQLIQEALIFDNKHTNYTMEHIRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMQEFRASFNHFDKDHGGALGPEEFKACLISLGYDVENDRQGEAEFNRIMSLVDPNHSGLVTFQAFIDFMSRETTDTDTADQVIASFKVLAGDKNFITAEELRRELPPDQAEYCIARMAPYQGPDAVPGALDYKSFSTALYGESDL
Protein: Meiotic recombination protein REC104 (P33323)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Potential transcriptional regulator that is required to activate expression of a number of early meiotic genes including HOP1.
Interaction partners:
- Meiotic recombination protein REC102
- Antiviral protein SKI8
- Meiosis-specific protein SPO11
- Meiotic recombination protein REC114
- Recombination protein 107
- Meiosis-specific protein MEI4
- Meiosis-specific protein HOP1
- Protein RED1
- Meiosis-specific protein SPO13
Sequence:
MSIEEEDTNKITCTQDFLHQYFVTERVSIQFGLNNKTVKRINKDEFDKAVNCIMSWTNYPKPGLKRTASTYLLSNSFKKSATVSLPFILGDPVCMPKRVESNNNDTCLLYSDTLYDDPLIQRNDQAGDEIEDEFSFTLLRSEVNEIRPISSSSTAQILQSDYSALMYERQASNGSIFQFSSP
Protein: Elongator complex protein 3 (EC 2.3.1.311) (tRNA uridine(34) acetyltransferase) (Q1ZXC6)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Catalytic tRNA acetyltransferase subunit of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (By similarity). In the elongator complex, acts as a tRNA uridine(34) acetyltransferase by mediating formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (By similarity).
Interaction partners:
- Elongator complex protein 1
- Elongator complex protein 4
- Elongator complex protein 2
- Cytoplasmic tRNA 2-thiolation protein 2
- Protein KTI12 homolog
- Cytoplasmic tRNA 2-thiolation protein 1
- Elongator complex protein 6
- Diphthamide biosynthesis protein 3
- DNA replication licensing factor mcm5
- Adenylyltransferase and sulfurtransferase MOCS3
Sequence:
MSLMNDPRPVSKKAGAKPVYGKNTPQFTKTVGEIVNALINAYKEGKKVNLLKIKTELAAKNSLSDQPKSVDIISAIPESYKNTLLPLLKAKPVRTASGIAVVAVMCKPHRCPHLAMTGNICVYCPGGPDSDFEYSTQSYTGYEPTSMRAIRARYNPFLQTRHRIDQLKRLGHNVEKVEFIIMGGTFMSLPSDYRDYFIRNLHDALSGHTSNNVAEAVKYSEQSNVKCVGITIETRPDHCLKLHLSNMLTYGCTRLEIGVQSVFEDIARDTNRGHTVRAVLESFQLAKDSGFKVVAHMMPDLPNMGMERDIYGFMEFFENPAFRADGLKIYPTLVIRGTGLYELWKTGTYKNYSPDSLVDLIAKVLALVPPWTRIYRIQRDIPMPLVTSGVEYGNLRELCLARMKDFGTKCRDVRTREVGIQEVHHKIKPDQVELIRRDYVANGGWETFLSFEDPKQDILIGLLRLRKCSETSFRPELKENCSIVRELHVYGSVVGIHNRDPTKFQHQGYGTLLMEEAERIAREEHGSIKLAVIAGVGTRHYYRKLGYELDGVYVSKYLG
Protein: Thiamine precursor transporter HmpT (Thiamine precursor ECF transporter S component HmpT) (A2RIH3)
Organism: Lactococcus lactis subsp. cremoris (strain MG1363)
Function: Probably a thiamine precursor-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. The substrates themselves are bound by transmembrane, not extracytoplasmic soluble proteins.
Subcellular location: Cell membrane {ECO:0000305|PubMed:21135102}; Multi-pass membrane protein {ECO:0000305|PubMed:21135102}.
Interaction partners:
- pyridoxal kinase
- Energy-coupling factor transporter ATP-binding protein EcfA1
- UPF0340 protein llmg_0465
- Energy-coupling factor transporter ATP-binding protein EcfA2
- Energy-coupling factor transporter transmembrane protein EcfT
- Pantothenic acid transporter PanT
- Putative aminotransferase
- Thiamine transporter ThiT
- Aminopyrimidine aminohydrolase
- Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase
Sequence:
MKLMDNKNIKKLTLLAIWTALTFVLGRLFTFPIPGSAGNILTLLDVGIYTAVFLFGKREAAIIGGFAAFLLDLTAGFSNYMFFSLIIHGGQGYLAGLTRYKWLNFLLSLLVMVGGYFIVGGLMYGWGSAIAGLWVNIVQVIVGFVLAKVLSPLIERTGILNGFRKA
Protein: Auxin response factor (A0A2H1ZEC0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU004561}.
Interaction partners:
Sequence:
METGNVVNAQPELSGIIDGSKSYMYEQLWKLCAGPLCDIPKLGENVYYFPQGNIELVDASTREELNELQPICDLPSKLQCRVIAIHLKVENNSDETYAEITLMPDTTQVVIPTQSENQFRPLVNSFTKVLTASDTSAYGGFFVPKKHAIECLPPLDMSQPLPAQELLAKDLHGNQWRFRHSYRGTPQRHSLTTGWNEFTTSKKLVKGDVIVFVRGETGELRVGIRRARHQQGNIPSSIVSIDCMRHGVIASAKHALDNQCIFIVVYKPRSSQFIVSYDKFLDAMNNKFIVGSRFTMRFEGDDFSERRYFGTIIGVNDFSPHWKCSEWRSLEVQWDEFASFSRPNKVSPWEIEHLMSALNVPRSSLLKNKRLREVNEFGQEIGQLSVASPMNTSLRYRDTTEDAMNPSRLLMSYPVQPMPKLNYNNQMVTQIEENITTKAVTNFRLFGVSLAIPLVIKDPIEEIGSDISKLTEGKKFGQSQTLRSPIEIQSKQFGSTRTCTKVQMQGVTIGRAVDLSVLNGYDQLILELEKLFDLKGQLQTRNQWKIAFTDSDGYEMLVGDDPWPEFCKMVKKILIYSKEEVKNLKSSKSLSS
Protein: Probable aminotransferase (EC 2.6.1.62) (Q7NWG4)
Organism: Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / CCUG 213 / NBRC 12614 / NCIMB 9131 / NCTC 9757 / MK)
Interaction partners:
- Agmatinase
- ATP-dependent dethiobiotin synthetase BioD
- Protoporphyrinogen oxidase
- Polyamine aminopropyltransferase
- Probable glutamine synthetase
- Biotin synthase
- Oxidoreductase
- Probable glutamine synthetase
- gamma-glutamyl-gamma-aminobutyrate hydrolase
- Probable alcohol dehydrogenase
Sequence:
MQKQRTTSQWRELDAAHHLHPFTDTASLNQAGARVMTRGEGVYLWDSEGNKIIDGMAGLWCVNVGYGRKDFAEAARRQMEELPFYNTFFKTTHPAVVELSSLLAEVTPAGFDRVFYTNSGSESVDTMIRMVRRYWDVQGKPEKKTLIGRWNGYHGSTIGGASLGGMKYMHEQGDLPIPGMAHIEQPWWYKHGKDMTPDEFGVVAARWLEEKILEIGADKVAAFVGEPIQGAGGVIVPPATYWPEIERICRKYDVLLVADEVICGFGRTGEWFGHQHFGFQPDLFTAAKGLSSGYLPIGAVFVGKRVAEGLIAGGDFNHGFTYSGHPVCAAVAHANVAALRDEGIVQRVKDDIGPYMQKRWRETFSRFEHVDDVRGVGMVQAFTLVKNKAKRELFPDFGEIGTLCRDIFFRNNLIMRACGDHIVSAPPLVMTRAEVDEMLAVAERCLEEFEQTLKARGLA
Protein: IKAROS family zinc finger 1 (A0A087WU46)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDADEGQDMSQVSVGKPHKCGYCGRSYKQRSSLEEHKERCHNYLESMGLPGTLYPVIKEETNHSEMAEDLCKIGSERSLVLDRLASNVAKRKSSMPQKFLGDKGLSDTPYDSSASYEKENEMMKSHVMDQAINNAINYLGAESLRPLVQTPPGGSEVVPVISPMYQLHKPLAEGTPRSNHSAQDSAVENLLLLSKAKLVPSEREASPSNSCQDSTDTESNNEEQRSGLIYLTNHIAPHARNGLSLKEEHRAYDLLRAASENSQDALRVVSTSGEQMKVYKCEHCRVLFLDHVMYTIHMGCHGFRDPFECNMCGYHSQDRYEFSSHITRGEHRFHMS
Protein: Isthmin-2 (Thrombospondin and AMOP domain-containing isthmin-like protein 1) (Thrombospondin type-1 domain-containing protein 3) (Q6H9L7)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Serine palmitoyltransferase 1
- Mucin-4
- Transforming growth factor beta-3 proprotein
Sequence:
MRALRDRAGLLLCVLLLAALLEAALGLPVKKPRLRGPRPGSLTRLAEVSASPDPRPLKEEEEAPLLPRTHLQAEPHQHGCWTVTEPAAMTPGNATPPRTPEVTPLRLELQKLPGLANTTLSTPNPDTQASASPDPRPLREEEEARLLPRTHLQAELHQHGCWTVTEPAALTPGNATPPRTQEVTPLLLELQKLPELVHATLSTPNPDNQVTIKVVEDPQAEVSIDLLAEPSNPPPQDTLSWLPALWSFLWGDYKGEEKDRAPGEKGEEKEEDEDYPSEDIEGEDQEDKEEDEEEQALWFNGTTDNWDQGWLAPGDWVFKDSVSYDYEPQKEWSPWSPCSGNCSTGKQQRTRPCGYGCTATETRTCDLPSCPGTEDKDTLGLPSEEWKLLARNATDMHDQDVDSCEKWLNCKSDFLIKYLSQMLRDLPSCPCAYPLEAMDSPVSLQDEHQGRSFRWRDASGPRERLDIYQPTARFCLRSMLSGESSTLAAQHCCYDEDSRLLTRGKGAGMPNLISTDFSPKLHFKFDTTPWILCKGDWSRLHAVLPPNNGRACTDNPLEEEYLAQLQEAKEY
Protein: Keratin, type II cytoskeletal 6B (Cytokeratin-6B) (CK-6B) (Keratin-6B) (K6B) (Type-II keratin Kb10) (P04259)
Organism: Homo sapiens (Human)
Interaction partners:
- Keratin, type I cytoskeletal 16
- Keratin, type II cytoskeletal 6A
- Keratin, type I cytoskeletal 17
- Keratin, type II cytoskeletal 5
- Keratin, type I cytoskeletal 14
- Desmoglein-3
- Keratin, type II cytoskeletal 6C
- Cornifin-B
- Proprotein convertase subtilisin/kexin type 5
Sequence:
MASTSTTIRSHSSSRRGFSANSARLPGVSRSGFSSISVSRSRGSGGLGGACGGAGFGSRSLYGLGGSKRISIGGGSCAISGGYGSRAGGSYGFGGAGSGFGFGGGAGIGFGLGGGAGLAGGFGGPGFPVCPPGGIQEVTVNQSLLTPLNLQIDPAIQRVRAEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQGTKTVRQNLEPLFEQYINNLRRQLDNIVGERGRLDSELRNMQDLVEDLKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRALYDAELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIAQRSRAEAESWYQTKYEELQITAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVKLALDVEIATYRKLLEGEECRLNGEGVGQVNISVVQSTVSSGYGGASGVGSGLGLGGGSSYSYGSGLGVGGGFSSSSGRATGGGLSSVGGGSSTIKYTTTSSSSRKSYKH
Protein: Bifunctional purine biosynthetic protein PUR2,5 (OpPUR2,5) [Includes: Phosphoribosylamine--glycine ligase (EC 6.3.4.13) (Glycinamide ribonucleotide synthetase) (GAR synthetase) (GARS) (Phosphoribosylglycinamide synthetase); Phosphoribosylformylglycinamidine cyclo-ligase (EC 6.3.3.1) (AIR synthase) (AIR synthetase) (AIRS) (Phosphoribosyl-aminoimidazole synthetase)] (G8EWC8)
Organism: Pichia angusta (Yeast) (Hansenula polymorpha)
Function: Catalyzes the second and fifth step in the 'de novo' purine biosynthesis pathway; contains phosphoribosylamine--glycine ligase (GARS) and phosphoribosylformylglycinamidine cyclo-ligase (AIRS) activities.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P20772}.
Interaction partners:
Sequence:
MEKINVLVVGNGGREHALVWKLAQSPWAKHIFVAPGNGGFSKLENVTSVPIGSSPSDFGSLVDFATKHNVGLVIPGPEQPLVDGITTWFQKAGIPVFGPSAKAARMEGSKTFSKDFMKKHNIPTARYENFTDYEAAKQYIANSSHNLVIKASGIAAGKGVLIPANKQEAYEAIKEIMVNKQFGSAGDEVVIEEFLEGDELSILCISDGYSFVDLPPAQDHKRIGDGDTGLNTGGMGAYSPAPIGTPSLLEKIRKNILKPTIDGMRKDGYPMVGCLFVGVMVTPDGDPKVLEYNVRFGDPETQTVLPLLKSDLLELMLATVEHRLDSVDFQVHADKYSTTVVVAAGGYPESYRKGDEITVKEPLPENTFIFHAGTKEENGKVVTAGGRVIAATAIADTLEEAVKKAYVGVDHISFKDKYNRTDIAHRAFKEKPKNKVSLTYEDAGVSVDAGNQLVEKIKKSVKSTKRPGADSEIGGFGGLFDLQRAGYTDINNTLLVAATDGVGTKLRVAQIMDIHNTVGIDLVAMNVNDLVVQGAEPLMFLDYFATAHLDIKVAADFVEGVADGCKLSGCALVGGETSEMPGMYAPGHYDTNGTAVGAVLKENILPKKDKMNAGDVLLGIASDGVHSNGFSLIRKIIETTDYSYTDPAPWNPKSTIGEEVLIPTRIYVKQLLPATRRGLILGLAHITGGGLVENIPRAIPDNLSAEVDMTTWNVPEIFKWLGKTGGVPINDILKTLNMGIGMVAIVKPENVEEVIKVLKEAGETVYTIGKLVERKDLPGCTIKNSEDLY