wanglab/gogpt-training-data huggingface dataset:
Protein: Cytochrome P450 2K1 (EC 1.14.14.1) (CYPIIK1) (Cytochrome P450 LMC2) (Q92090)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Microsome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MSLIEDILQTSSTVTLLGTVLFLLVLYLRSSGSSSEEQGKEPPGPRPLPLLGNMLQLDLKKPYCTLCELSKKYGSIFTVHFGPKKVVVLAGYKTVKQALVNQAEDFGDRDITPVFYDFNQGHGILFANGDSWKEMRRFALTNLRDFGMGKKGSEEKILEEIPYLIEVFEKHEGKAFDTTQSVLYAVSNIISAIVYGSRFEYTDPLFTGMADRAKESIHLTGSASIQMYNMFPWLGPWINNLTRLKKNIADMKMEVIELVRGLKETLNPHMCRGFVDSFLVRKQTLEESGHMDSFYHDDNLVFSVGNLFSAGTDTTGTTLRWGLLLMTKYPHIQDQVQEEISRVIGSRQTLVEDRKNLPYTDAVIHETQRLANIVPMSVPHTTSRDVTFQGYFIKKGTSVIPLLTSVLQDDSEWESPNTFNPSHFLDEQGGFVKRDAFMAFSAGRRVCLGEGLARMELFLFFTSLLQRFRFSPPPGVTEDDLDLTPLLGFTLNPSPHQLCAVSRV
Protein: Ankyrin repeat-containing protein 2 (F4JN13)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MASNSEKNPLLSDEKPKSTEENKSSKPESASGSSTSSAMPGLNFNAFDFSNMASILNDPSIREMAEQIAKDPAFNQLAEQLQRSIPNAGQEGGFPNFDPQQYVNTMQQVMHNPEFKTMAEKLGTALVQDPQMSPFLDAFSNPETAEHFTERMARMKEDPELKPILDEIDAGGPSAMMKKNYLFCFRYWNDPEVLKKLGEAMGMPVAGLPDQTVSAEPEVAEEGEEEESIVHQTASLGDVEGLKAALASGGNKDEEDSEGRTALHFACGYGELKCAQVLIDAGASVNAVDKNKNTPLHYAAGYGRKECVSLLLENGAAVTLQNLDEKTPIDVAKLNSQLEVVKLLEKDAFL
Protein: Testicular secretory protein Li 54 (A0A140VK54)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSDHGDVSLPPEDRVRALSQLGSAVEVNEDIPPRRYFRSGVEIIRMASIYSEEGNIEHAFILYNKYITLFIEKLPKHRDYKSAVIPEKKDTVKKLKEIAFPKAEELKAELLKRYTKEYTEYNEEKKKEAEELARNMAIQQELEKEKQRVAQQKQQQLEQEQFHAFEEMIRNQELEKERLKIVQEFGKVDPGLGGPLVPDLEKPSLDVFPTLTVSSIQPSDCHTTVRPAKPPVVDRSLKPGALSNSESIPTIDGLRHVVVPGRLCPQFLQLASANTARGVETCGILCGKLMRNEFTITHVLIPKQSAGSDYCNTENEEELFLIQDQQGLITLGWIHTHPTQTAFLSSVDLHTHCSYQMMLPESVAIVCSPKFQETGFFKLTDHGLEEISSCRQKGFHPHSKDPPLFCSCSHVTVVDRAVTITDLR
Protein: Flavin carrier protein 2 (FAD transporter 2) (TRP-like ion channel FLC2) (P39719)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May be responsible for the transport of FAD into the endoplasmic reticulum lumen, where it is required for oxidative protein folding.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16717099}; Multi-pass membrane protein {ECO:0000269|PubMed:16717099}.
Interaction partners:
- Protein KRE1
- Mannan endo-1,6-alpha-mannosidase DFG5
- Flavin carrier protein 1
Sequence:
MIFLNTFARCLLTCFVLCSGTARSSDTNDTTPASAKHLQTTSLLTCMDNSQLTASFFDVKFYPDNNTVIFDIDATTTLNGNVTVKAELLTYGLKVLDKTFDLCSLGQVSLCPLSAGRIDVMSTQVIESSITKQFPGIAYTIPDLDAQVRVVAYAQNDTEFETPLACVQAILSNGKTVQTKYAAWPIAAISGVGVLTSGFVSVIGYSATAAHIASNSISLFIYFQNLAITAMMGVSRVPPIAAAWTQNFQWSMGIINTNFMQKIFDWYVQATNGVSNVVVANKDVLSISVQKRAISMASSSDYNFDTILDDSNLYTTSEKDPSNYSAKILVLRGIERVAYLANIELSNFFLTGIVFFLFFLFVVVVSLIFFKALLEVLTRARILKETSNFFQYRKNWGSIIKGTLFRLSIIAFPQVSLLAIWEFTQVNSPAIVVDAVVILLIITGLLVYGTIRVFIKGRESLRLYKNPAYLLYSDTYFLNKFGFLYVQFKADKFWWLLPLLSYAFLRSLFVAVLQNQGKAQAMIIFVIELAYFVCLCWIRPYLDKRTNVFNIAIHLVNLINAFFFLFFSNLFKQPAVVSSVMAVILFVLNAVFALFLLLFTIVTCTLALLHRNPDVRYQPMKDDRVSFIPKIQNDFDGKNKNDSELFELRKAVMDTNENEEEKMFRDDTFGKNLNANTNTARLFDDETSSSSFKQNSSPFDASEVTEQPVQPTSAVMGTGGSFLSPQYQRASSASRTNLAPNNTSTSSLMKPESSLYLGNSNKSYSHFNNNGSNENARNNNPYL
Protein: Regulator of chromosome condensation (Cell cycle regulatory protein) (RCC1 homolog) (Q18211)
Organism: Caenorhabditis elegans
Function: Key component of the Ran GTPase system, which comprises ran-1, ran-2 and ran-3 and is essential in nucleocytoplasmic transport. Promotes the exchange of Ran-bound GDP by GTP and regulates the onset of chromosome condensation in the S phase. Binds to the chromatin. RCC1 (ran-3)/RAN (ran-1) complex (together with other proteins) acts as a component of a signal transmission pathway that detects unreplicated DNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:11909538}.
Interaction partners:
- GTP-binding nuclear protein ran-1
- Ran GTPase-activating protein 2
- Nuclear Pore complex Protein
- Importin subunit alpha-3
- Importin subunit alpha-2
- Phosphodiesterase delta-like protein
- RNA cytidine acetyltransferase
- Importin subunit alpha
- RanBD1 domain-containing protein
- Structural maintenance of chromosomes protein 4
Sequence:
MSTAEQRMDTSEVELPNDNVNEQGNKTPRADQPESSASGARNHGEDEEVTEQVELAAMETEASDSIVDNVPKTPRRAGRPKKLPSTSTAAAESAVTPGKRGRKRKGSESVNTTINSTMNSTLNEPKTPGRKQAKLVAPLLTYDLFAPSIIGDRVLSCGEGEALGHPGRTTTKKPRKVDIFEEEGLKPLQAVAGGVHSAVLTSEGEVYMCGINEKGTVPAEGVEKEGSTDEFAKVKFEEDIEKEGKIVMLAAGASFTAALTDQGSVIAWGNLRNSNGNVDVHPLLHKMQEAPVVIVHQAKRKIVKIAAGENHLVMLDEKGCLLTFGDGEMGQLGRSSRTKTIRSKYMCDESGDHLLVPLRFKHKGKFFDVVAKNVFASGFWTIVHGEDGKYYAFGLNNYAQLGIKVDEADVGQDGQDNRELRVFLPAEAPAFGAERTFVNIEGVQHVVILGSDGKVFAMGKNTDNALGLGNWTGKDDQQHWLYDTIQEIEFDSKIVGVSAKLATSIAWSEDGTAYAWGFDTTGQLGLGLKDEDEKMVSKPEEISSAHLDGYSIIGASISDQHTLIIAKKN
Protein: F-actin-capping protein subunit beta (Q9HGP5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Competes with formin cdc12 for attachment to the actin filaments barbed ends. Slowly replaces cdc12 on the barbed ends in preparation for filament disassembly during contractile ring constriction.
Subcellular location: Cytoplasm, cytoskeleton, actin patch {ECO:0000250|UniProtKB:P13517}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15743909}. Nucleus {ECO:0000269|PubMed:16823372}. Note=Cell division site. Localizes to cell tips during interphase. {ECO:0000269|PubMed:16823372}.
Interaction partners:
- F-actin-capping protein subunit alpha
- Twinfilin
- Fimbrin
- Centractin
- Actin-like protein arp10
- Uncharacterized WD repeat-containing protein C9G1.05
- Actin
- Uncharacterized protein C16C6.04
- Actin-related protein 3
- Protein app1
Sequence:
MNSEDAALDLLRRLNPKDISKNLDTILSVAPDLADVLLSSVDQPLKVNTCSESGNQYLLCDFNRDGDSYRSPWSNKYDPPLEDGLVSTDRVRKLEVSLNEAIRVYLDLYYEGGVSSVYLWDQDDSYAGAVLIKKASTSNSSGWDSIHVFECLPTTETNVYDYRLTSTIILFLSSGSEEQSALPSKALNLSGHLTRQTSQRLPAADDDTEIANVGKLVEEMETRMRNFLQDVYFGKTKDIINQTRSIQPVSDAQPNDSALRSVLNDLSI
Protein: Pickel, isoform D (Q2PE37)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRELNKQQSQDTTDSGVEKGDYPRATNGVVFGAIVTFASFFVLMMSFCSPYWIESYEETRASFKNMGLWQYCFKDFVYPKYAFLKQFTGCHNIFSHVSTANWPVLILVLIFSHSYRSITLSVSICCPAGSWRCRAS
Protein: Secreted aspartic protease 1 (ACP 1) (Aspartate protease 1) (EC 3.4.23.24) (Candidapepsin-1) (Pepsinogen-1) (Pepsinogen-10) (P0CY27)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Secreted aspartic peptidases (SAPs) are a group of ten acidic hydrolases considered as key virulence factors. These enzymes supply the fungus with nutrient amino acids as well as are able to degrade the selected host's proteins involved in the immune defense. Induces host inflammatory cytokine production in a proteolytic activity-independent way. Plays a role in tissue damage during superficial infection. Moreover, acts toward human hemoglobin though limited proteolysis to generate a variety of antimicrobial hemocidins, enabling to compete with the other microorganisms of the same physiological niche using the microbicidal peptides generated from the host protein.
Subcellular location: Secreted {ECO:0000269|PubMed:11065355, ECO:0000269|PubMed:8478090, ECO:0000269|PubMed:9841840}.
Interaction partners:
- ATP-dependent RNA helicase DBP6
Sequence:
MFLKNIFIALAIALLVDASPAKRSPGFVTLDFDVIKTPVNATGQEGKVKRQAIPVTLNNEHVSYAADITIGSNKQKFNVIVDTGSSDLWVPDASVTCDKPRPGQSADFCKGKGIYTPKSSTTSQNLGTPFYIGYGDGSSSQGTLYKDTVGFGGASITKQVFADITKTSIPQGILGIGYKTNEAAGDYDNVPVTLKNQGVIAKNAYSLYLNSPNAATGQIIFGGVDKAKYSGSLIAVPVTSDRELRITLNSLKAVGKNINGNIDVLLDSGTTITYLQQDVAQDIIDAFQAELKSDGQGHTFYVTDCQTSGTVDFNFDNNAKISVPASEFTAPLSYANGQPYPKCQLLLGISDANILGDNFLRSAYLVYDLDDDKISLAQVKYTSASNIAALT
Protein: Holocytochrome c-type synthase (EC 4.4.1.17) (A0A1D8PN32)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273, ECO:0000256|RuleBase:RU363130}.
Interaction partners:
- Protoheme IX farnesyltransferase, mitochondrial
- Holocytochrome c-type synthase
- Ferrochelatase
- Ubiquitin-conjugating enzyme E2 6
- Cytochrome c
Sequence:
MGWFWADKPSQDTVKATSFFTTPSACPIDHSKLASSSPTCPVKLNNDNDEVLNPLNNMPMAISSERAPGQRIKLSTERTISTIPRGESEDQGLWEYPSPQQMLNAMLSKGKGDGVPEDAVESMVEVHNFLNEGAWQQILTWEDQYTQQTKVEPRLKKFTGRPHDLSPKARMYLWLGQLFPETFNTIPPFDRHDWTVLRSCGRNQGWKEVRYVIDYYGAPDDEETGMPAFMLDTRPALDNLTNARDRFTHWAYPLWKKAMGEVRD
Protein: Corticoliberin (Corticotropin-releasing factor) (CRF) (Corticotropin-releasing hormone) (P01143)
Organism: Rattus norvegicus (Rat)
Function: Hormone regulating the release of corticotropin from pituitary gland. Induces NLRP6 in intestinal epithelial cells, hence may influence gut microbiota profile (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:6603620}.
Interaction partners:
- Corticotropin-releasing factor receptor 1
- Corticotropin-releasing factor receptor 2
- Corticotropin-releasing factor-binding protein
- Urocortin-2
- Urocortin
- Urocortin 3.
- Pro-opiomelanocortin
- Pro-neuropeptide Y
- Oxytocin-neurophysin 1
- Pro-thyrotropin-releasing hormone
Sequence:
MRLRLLVSAGMLLVALSPCLPCRALLSRGSVSGAPRAPQPLNFLQPEQPQQPQPILIRMGEEYFLRLGNLNRSPAARLSPNSTPLTAGRGSRPSHDQAAANFFRVLLQQLQMPQRPLDSSTELAERGAEDALGGHQGALERERRSEEPPISLDLTFHLLREVLEMARAEQLAQQAHSNRKLMEIIGK
Protein: Ribosomal protein uS12 methylthiotransferase RimO (uS12 MTTase) (uS12 methylthiotransferase) (EC 2.8.4.4) (Ribosomal protein uS12 (aspartate(89)-C(3))-methylthiotransferase) (Ribosome maturation factor RimO) (P0AEI4)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the methylthiolation of the residue Asp-89 of ribosomal protein S12.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Dual-specificity RNA methyltransferase RlmN
- Ribosomal protein S12 methylthiotransferase accessory factor YcaO
- Signal peptidase I
- Biotin synthase
- HTH-type transcriptional repressor PurR
- Glutamine--tRNA ligase
- DNA topoisomerase 4 subunit A
- Outer-membrane lipoprotein LolB
- Elongation factor Tu 2
- Elongation factor Tu 1
Sequence:
MSKVTPQPKIGFVSLGCPKNLVDSERILTELRTEGYDVVPSYDDADMVIVNTCGFIDSAVQESLEAIGEALNENGKVIVTGCLGAKEDQIREVHPKVLEITGPHSYEQVLEHVHHYVPKPKHNPFLSLVPEQGVKLTPRHYAYLKISEGCNHRCTFCIIPSMRGDLVSRPIGEVLSEAKRLVDAGVKEILVISQDTSAYGVDVKHRTGFHNGEPVKTSMVSLCEQLSKLGIWTRLHYVYPYPHVDDVIPLMAEGKILPYLDIPLQHASPRILKLMKRPGSVDRQLARIKQWREICPELTLRSTFIVGFPGETEEDFQMLLDFLKEARLDRVGCFKYSPVEGADANALPDQVPEEVKEERWNRFMQLQQQISAERLQEKVGREILVIIDEVDEEGAIGRSMADAPEIDGAVYLNGETNVKPGDILRVKVEHADEYDLWGSRV
Protein: Uptake hydrogenase small subunit (EC 1.12.99.6) (Hydrogenlyase) (Membrane-bound hydrogenase small subunit) (P31892)
Organism: Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337) (Ralstonia eutropha)
Function: This enzyme recycles the H(2) produced by nitrogenase to increase the production of ATP and to protect nitrogenase against inhibition or damage by O(2) under carbon- or phosphate-limited conditions.
Subcellular location: Cell membrane; Peripheral membrane protein.
Interaction partners:
Sequence:
MVETFYEVMRRQGISRRSFLKYCSLTATSLGLGPSFLPQIAHAMETKPRTPVLWLHGLECTCCSESFIRSAHPLAKDVVLSMISLDYDDTLMAAAGHQAEAILEEIMTKYKGNYILAVEGNPPLNQDGMSCIIGGRPFIEQLKYVAKDAKAIISWGSCASWGCVQAAKPNPTQATPVHKVITDKPIIKVPGCPPIAEVMTGVITYMLTFDRIPELDRQGRPKMFYSQRIHDKCYRRPHFDAGQFVEEWDDESARKGFCLYKMGCKGPTTYNACSTTRWNEGTSFPIQSGHGCIGCSEDGFWDKGSFYDRLTGISQFGVEANADKIGGTASVVVGAAVTAHAAASAIKRASKKNETSGSEH
Protein: Uncharacterized protein YGL230C (P53074)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- ER membrane protein complex subunit 4
- Translation initiation factor eIF2B subunit beta
- SIT4-associating protein SAP4
- Translation initiation factor eIF2B subunit gamma
- tRNA acetyltransferase TAN1
Sequence:
MGIITLSGNVLHLLKAYPKKGLEEVSQPEPNTANDSSTEYKGKSKDDFQMVEKSNTDERYNFTRTKKWFLLMTSEYYKLMENRLLMFCIIACSFICAIQFLFFIIYWTNIVPRKTQRAITNLNYDYLTAHLKEQCVPYAKILDQCIL
Protein: GTP-binding protein gtr1 (EC 3.6.5.-) (O74824)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: GTPase involved in activation of the TORC1 signaling pathway, which promotes growth and represses autophagy in nutrient-rich conditions (By similarity). Also required for TORC1 inactivation during nitrogen starvation (By similarity).
Subcellular location: Vacuole membrane {ECO:0000250|UniProtKB:A0A6A5PR12}; Peripheral membrane protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- GTP-binding protein gtr2
- Serine/threonine-protein kinase tor2
- Nitrogen permease regulator 2 homolog
- Target of rapamycin complex 1 subunit mip1
- Uncharacterized protein C1778.05c
- Nitrogen permease regulator 3-like protein
- Uncharacterized WD repeat-containing protein C4F8.11
- Serine/threonine-protein kinase tor1
- Uncharacterized WD repeat-containing protein C12G12.01c
- Vacuolar membrane-associated protein iml1
Sequence:
MRKKVLLMGRSGSGKSSMRSIVFSNYVAKDTRRLGATIDIEHSHVRFLGNLVLNLWDCGGQEAFMENYLSAQRDHIFRNVQVLIYVFDVESREFERDLVTFRNCLEATVANSPQARVFCLIHKMDLVQEDLRDLVFEERKAILLETSKDLETTCLATSIWDETLFKAWSAIVYTLIPNTPTLESHLREFAKAAEAAEVILFERTTFLVISSYSSESNPATDAHRFEKISNIVKQFKLSCSKMQAQFTTFELRGGNFSAFIVPYTEDTYILVVIADPEIESAVTLMNIQSARRFIEASKSASDGIQLQP
Protein: UDP-N-acetylglucosamine transferase subunit alg13 (EC 2.4.1.141) (Asparagine-linked glycosylation protein 13) (O14190)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway (By similarity).
Subcellular location: Endoplasmic reticulum {ECO:0000250}.
Interaction partners:
- UDP-N-acetylglucosamine transferase subunit alg14
- Chitobiosyldiphosphodolichol beta-mannosyltransferase
- GDP-Man:Man
- UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
- Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Probable dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Probable Dol-P-Man:Man
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit stt3
- Uncharacterized protein C553.06
- Dolichyl-phosphate beta-glucosyltransferase
Sequence:
MNAFVTVGSTQFDDLIRAVLKPEFQHCLVKHGINQLIVQYGKGKQAFGDPKSVAGLTILGFDYAPEIESYIHDASIVISHAGAGSILQTLRSGKRLLVVPNESLMDNHQVELATKLASMNYLVTCSTSNLVEGLEELYPKILTPFPKSDCSTFQKVMQDVAR
Protein: Transcription factor MYB72 (Myb-related protein 72) (AtMYB72) (Q9SGU3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in metal ions homeostasis, including iron ions (Fe) acquisition, via the regulation of NAS4 and NAS2 genes expression. Necessary for plant survival in alkaline soil where iron availability is greatly restricted. Involved in the up-regulation of several biosynthesis genes of secondary metabolites involved in iron uptake under conditions of iron deficiency. Triggers tolerance to nickel (Ni) and zinc (Zn) ions. Required in the roots during early signaling steps of rhizobacteria-mediated (e.g. P.fluorescens WCS417r) and beneficial fungi-mediated (e.g. T.asperellum T34) broad-spectrum induced systemic resistance (ISR) against several pathogens (e.g. P.syringae pv tomato, H.parasitica, P.cucumerina, A.brassicicola and B.cinerea) and implying enhanced callose deposition. Required for the induction of some genes (e.g. BGLU42) upon rhizobacteria-mediated ISR.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:24278034}.
Interaction partners:
- Beta-glucosidase 42
- Fe
- Ferric reduction oxidase 2
- Probable nicotianamine synthase 4
- Scopoletin 8-hydroxylase
- Feruloyl CoA ortho-hydroxylase 1
- Transcription factor ORG3
- Xanthotoxin 5-hydroxylase CYP82C4
- Transcription factor bHLH47
- Transcription factor bHLH101
Sequence:
MGKGRAPCCDKNKVKRGPWSPQEDLTLITFIQKHGHQNWRSLPKLAGLLRCGKSCRLRWINYLRPDVKRGNFSKKEEDAIIHYHQTLGNKWSKIASFLPGRTDNEIKNVWNTHLKKRLTPSSSSSSLSSTHDQSTKADHDKNCDGAQEEIHSGLNESQNSATSSHHQGECMHTKPELHEVNGLNEIQFLLDHDDFDDITSEFLQDNDILFPLDSLLHNHQTHISTQEMTREVTKSQSFDHPQPDIPCGFEDTNEESDLRRQLVESTTPNNEYDEWFNFIDNQTYFDDFNFVGEVCL
Protein: SUEL-type lectin domain-containing protein (A0A060XUW4)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
- ZU5 domain-containing protein
- Ig-like domain-containing protein
- Uncharacterized protein
- Netrin receptor UNC5
- Uncharacterized protein
- Netrin receptor UNC5
- ZU5 domain-containing protein
- UPA domain-containing protein
- Death domain-containing protein
- Netrin receptor UNC5
Sequence:
MSCPNQFRVTSRCDGNEKCDVATSGSVCDLCSTAYLTNIFLDVTYGCLESKKVTTCHGVVHLECGDGVVFLQKALYGRIDSQTCSQGRPQSELTNTKCSQEGTLALWSQRCDGKQTCEVNMRVNQISDPCVGTYKYLDVTYICLPAKTSITCEGSTSSLDCGKGVIKVFHANYGRRDGSTCSAGRHELSNQNCLQPKTLDVVKQWCEGKSQCTVGLDPVFGDPCYGTYKYLEVSYTCLGVSPTV
Protein: F-box protein MET30 (E3 ubiquitin ligase complex SCF(Met30) subunit MET30) (Methionine-requiring protein 30) (P39014)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Substrate-recognition component of the SCF(Met30) complex, an E3 ubiquitin ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Negatively regulates sulfur amino acids biosynthesis genes expression. Controls cell cycle function (being required for the G1/S transition and M-phase but not the S-phase), sulfur metabolism, and methionine biosynthesis as part of the SCF(Met30) complex. Required for the efficient binding of CDC45 and MCM proteins to origins of replication. Required for efficient expression of G1 cyclins. The SCF(Met30) complex catalyzes ubiquitination and degradation of the Cdk-inhibitory kinase SWE1. Involved in the S-adenosylmethionine (AdoMet)-mediated inhibition of the transcription function of MET4. The SCF(Met30) complex mediates ubiquitination and subsequent degradation of MET4 and the cellular response to cadmium. The SCF(Met30) complex acts as an inhibitor of autophagy by promoting ubiquitination and degradation of ATG9 in normal conditions.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14660673}. Nucleus {ECO:0000269|PubMed:10637232, ECO:0000269|PubMed:14660673}.
Interaction partners:
- Suppressor of kinetochore protein 1
- Cell division control protein 53
- Transcriptional activator of sulfur metabolism MET4
- RING-box protein HRT1
- SCF E3 ubiquitin ligase complex F-box protein GRR1
- Transcriptional regulator MET32
- Mitosis inhibitor protein kinase SWE1
- Ubiquitin-conjugating enzyme E2-34 kDa
- Cell division control protein 4
- E3 ubiquitin-protein ligase complex SLX5-SLX8 subunit SLX5
Sequence:
MRRERQRMMSFEDKDKDDLDNSNSNNSSEMTDTAMMPPLKRLLITGSSDDLAQGSSGKKKMTMATRSPSSSPDLATNDSGTRVQPLPEYNFTKFCYRHNPDIQFSPTHTACYKQDLKRTQEINANIAKLPLQEQSDIHHIISKYSNSNDKIRKLILDGILSTSCFPQLSYISSLVTHMIKIDFISILPQELSLKILSYLDCQSLCNATRVCRKWQKLADDDRVWYHMCEQHIDRKCPNCGWGLPLLHMKRARIQQNSTGSSSNADIQTQTTRPWKVIYRERFKVESNWRKGHCRIQEFKGHMDGVLTLQFNYRLLFTGSYDSTIGIWDLFTGKLIRRLSGHSDGVKTLYFDDRKLITGSLDKTIRVWNYITGECISTYRGHSDSVLSVDSYQKVIVSGSADKTVKVWHVESRTCYTLRGHTEWVNCVKLHPKSFSCFSCSDDTTIRMWDIRTNSCLKVFRGHVGQVQKIIPLTIKDVENLATDNTSDGSSPQDDPTMTDGADESDTPSNEQETVLDENIPYPTHLLSCGLDNTIKLWDVKTGKCIRTQFGHVEGVWDIAADNFRIISGSHDGSIKVWDLQSGKCMHTFNGRRLQRETQHTQTQSLGDKVAPIACVCIGDSECFSGDEFGCVKMYKFDLND
Protein: Cyclin E2 (A0A8I6A291)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSRRSRLQAKQQHARPNQPDSPQEAQIIQAKKRKTAQDVKKRTEEITKKHQYEIRNCWPPVLSGGISPCIIIETPHKEIGTSDFSRFTNYRFKNLFINPSPLPDLSWACSQEVWQNMLQKESRYVHDKHFEVLHSDLEPQMRSILLDWLLEVCEVYTLHRETFYLAQDFFDRFMLTQKDVNKNMLQLIGITSLFIASKLEEIYAPKLQEFAYVTDGACSEVDILKMELNILKALKWELCPVTVISWLNLFLQVDAVKDIPKVLLPQYSQETFIQIAQLLDLCILAIDSLEFQYRILAAAALCHFTSIEVVKKASGLEWDDISECVDWMVPFVSVVKSVSPVKLKTFKKIPMEDRHNIQTHTNYLALLNEVNYVNIFRKGGQLSPVCNGGIMTPPKSTEKPPVKF
Protein: Adaptive-response sensory kinase SasA (EC 2.7.13.3) (Sensor histidine kinase SasA) (Synechococcus adaptive sensor protein A) (SasA) (Q06904)
Organism: Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805) (Anacystis nidulans R2)
Function: Member of the two-component regulatory system SasA/RpaA involved in genome-wide circadian gene expression. One of three clock output pathways. Participates in the KaiABC clock protein complex, which constitutes the main circadian regulator in cyanobacteria, via its interaction with KaiC. Required for robustness of the circadian rhythm of gene expression and involved in clock output. KaiC enhances the autophosphorylation activity of SasA, which then transfers its phosphate group to RpaA to activate it. Phosphotransfer is maximal when KaiC phosphorylation is active during the circadian cycle; this two-component system is activated by fully phosphorylated KaiC. A very robust clock is reconstituted with KaiA, KaiB, KaiC, SasA, CikA and RpaA; output is measured by transcription from an appropriate reporter. In addition to its output function, recruits fold-shifted KaiB (KaiB(fs)) to KaiC to cooperatively form the KaiB(6):KaiC(6) complex (independent of SasA kinase activity); at physiological concentrations increases their association. At higher concentrations SasA and KaiB(fs) compete to bind to KaiC. Mutations that decrease cooperativity nearly phenocopy a deletion mutation.
Interaction partners:
- DNA-binding dual master transcriptional regulator RpaA
- Circadian clock oscillator protein KaiC
- Response regulator receiver domain protein
- Two component transcriptional regulator, LuxR family
- Probable transcriptional regulator ycf27
- Probable transcriptional regulator ycf27
- Potassium-transporting ATPase D chain
- Diguanylate cyclase with GAF sensor
- histidine kinase
- Two component transcriptional regulator, winged helix family
Sequence:
MGESLSPQALAQPLLLQLFVDTRPLSQHIVQRVKNILAAVEATVPISLQVINVADQPQLVEYYRLVVTPALVKIGPGSRQVLSGIDLTDQLANQLPQWLVQQEAFFADREPPEVNIPFTELGQPETPALQQADAFFQLQQQYADLSERTKFLEQVIALVAHDLRNPLTAALLAVDTIQIRSQSFSVATAKEMQGLCSLFDQARSQLREIERMIAEILEATRHSGESLRINPREVVFEPLLQQVLEQLHERWRSKQQQLITDVPGDLPTLYADPDRLRQVLVNLLDNAIKYTPPGGTITIAALHRTSQKVQISISDTGSGIPRDQLSVIFKNLVRLSRDSSQEGYGIGLSVCQRIVQAHFGRIWVASELGQGSTFHFTMPVYRYTMPC
Protein: ATP-dependent DNA helicase Rep (EC 5.6.2.4) (DNA 3'-5' helicase Rep) (P09980)
Organism: Escherichia coli (strain K12)
Function: Rep helicase is a single-stranded DNA-dependent ATPase involved in DNA replication; it can initiate unwinding at a nick in the DNA. It binds to the single-stranded DNA and acts in a progressive fashion along the DNA in the 3' to 5' direction.
Interaction partners:
- Beta sliding clamp
- ATP-dependent DNA helicase RecQ
- Replicative DNA helicase DnaB
- UvrABC system protein B
- Protein CbrA
- DNA polymerase III subunit alpha
- Protein RecA
- Chromosomal replication initiator protein DnaA
- UvrABC system protein C
Sequence:
MRLNPGQQQAVEFVTGPCLVLAGAGSGKTRVITNKIAHLIRGCGYQARHIAAVTFTNKAAREMKERVGQTLGRKEARGLMISTFHTLGLDIIKREYAALGMKANFSLFDDTDQLALLKELTEGLIEDDKVLLQQLISTISNWKNDLKTPSQAAASAIGERDRIFAHCYGLYDAHLKACNVLDFDDLILLPTLLLQRNEEVRKRWQNKIRYLLVDEYQDTNTSQYELVKLLVGSRARFTVVGDDDQSIYSWRGARPQNLVLLSQDFPALKVIKLEQNYRSSGRILKAANILIANNPHVFEKRLFSELGYGAELKVLSANNEEHEAERVTGELIAHHFVNKTQYKDYAILYRGNHQSRVFEKFLMQNRIPYKISGGTSFFSRPEIKDLLAYLRVLTNPDDDSAFLRIVNTPKREIGPATLKKLGEWAMTRNKSMFTASFDMGLSQTLSGRGYEALTRFTHWLAEIQRLAEREPIAAVRDLIHGMDYESWLYETSPSPKAAEMRMKNVNQLFSWMTEMLEGSELDEPMTLTQVVTRFTLRDMMERGESEEELDQVQLMTLHASKGLEFPYVYMVGMEEGFLPHQSSIDEDNIDEERRLAYVGITRAQKELTFTLCKERRQYGELVRPEPSRFLLELPQDDLIWEQERKVVSAEERMQKGQSHLANLKAMMAAKRGK