wanglab/gogpt-training-data huggingface dataset:
Protein: Protein-S-isoprenylcysteine O-methyltransferase (EC 2.1.1.100) (Isoprenylcysteine carboxylmethyltransferase) (Prenylated protein carboxyl methyltransferase) (PPMT) (Prenylcysteine carboxyl methyltransferase) (pcCMT) (Q9EQK7)
Organism: Mus musculus (Mouse)
Function: Catalyzes the post-translational methylation of isoprenylated C-terminal cysteine residues.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O60725}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O60725}.
Interaction partners:
- CAAX prenyl protease 2
- CAAX prenyl protease 1 homolog
- GTPase HRas
- GTPase NRas
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- GTPase KRas
- Protein farnesyltransferase subunit beta
Sequence:
MAAARRGSAGSEARLSLATFLLGASVLALPLLTRAGLQGRTGLALYVAGLNALLLLLYRPPRYQIAIRACFLGFVFGCGVLLSFSQSSWNHFGWYVCSLSLFHYSEYLVTAVNNPKSLSLDSFLLNHSLEYTVAALSSWIEFTLENIFWPELKQITWLSATGLLMVVFGECLRKAAMFTAGSNFNHVVQSEKSDTHTLVTSGVYAWCRHPSYVGWFYWSIGTQVMLCNPICGVVYALTVWRFFRDRTEEEEISLIHFFGEEYLDYKKRVPTGLPFIKGVKVEL
Protein: Glucosylceramidase (EC 3.2.1.45) (E7EZM1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Lysosome membrane {ECO:0000256|ARBA:ARBA00004207}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004207}; Lumenal side {ECO:0000256|ARBA:ARBA00004207}.
Interaction partners:
- Non-lysosomal glucosylceramidase
- Sphingomyelin phosphodiesterase
- N-acylsphingosine amidohydrolase
- Beta-galactosidase.
- Acid ceramidase
- Galactocerebrosidase
- UDP-glucose ceramide glucosyltransferase.
- Ceramide kinase
- Beta-galactosidase-1-like protein precursor
- Galactosylceramidase b.
Sequence:
MRETALFILLAGIITTARADSKDGCLALNFGHGSVVCVCNATYCDSLGRTVLPDAGQFLSYVSNKAGSRLMESQGQFQKNSTGAALRITLNPSQKFQHIKGFGGAMTDAAAINILSLSSGAQDQLLRQYFSTDGIEYRFVRVPVASCDFSTRLYTYADTPEDYDLQNFTLAKEDVHMKIPLLQRAQALSAQPLYLFASAWSAPAWLKTNGALIGKGSLKGKPGGKEHKTWAQYYIRFLEEYRKYNLSFWGLTSGNEPTAGEMTNYSFQALGFTPETQRDWIALDLGPALHSSSFSKTQLMILDDNRLMLPHWAKVVLSDIKAARYVHGIGVHWYFDRLVPPDVTLTSTHHLYPDYFLFATEACAGWSPVDRGVRLGSWDRAEDYAHDIIQDLNNYVTGWTDWNLALNQDGGPNWVKNFVDSPIIVDPSKDIFYKQPTFYSMAHFSKFLWEESQRVGVSFSQQTSLEMSAFIRPDASAVLIILNRSEEEVPFEVWDQTVGFLPGSAPPHSILTLLWNRQ
Protein: EG:23E12.2 protein (O96833)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQYKKAIHATLTTSQPVIREEEENTIFFKIDELYDLHTGFLSDLKTIVSHEGGDVLIGEPFRRLAEMFDLYSAFLHNYKNAIETVKKCSANNPQFKKIVSTIVLNLQTEQSLTLEDLLHKPVARVQINALVFNDLLRETPNAHPDHQPLRQAQKIIQMFLNQFNVVNQRLPIESNRNLRRMVRNSFIVELVDGHRKLRHLFLFNDVIACAKYKALGRDRIDYELKWFIPLKDVSIYEEADPAVELKESSPANISQVKRNLRSVRDQLAMEVANSGSGGFRSGDKYRRKLADLESQLVLATPNLVLRLGNKANNKTITFFLSSDFERTQWIDSILSLKQKCNLPGANTINSLEVTAFIVAMQKGMKTEMGSYLMRNTNDESLLVGDLYMGVHGLEGLEQANDLYICVEVDSYGHYFRKATTKKICRSQTPLWNESFMLELEGSQNVRILLYEAKERPLLKAKHILKVGVKSACIREVERRGMLEVGCYRVSGSASDLAKLKKAFESGEYMALMDAYEAEQLLREVDIHSVTGILKTFLRELPEALFTDQLYPRFFDTFSAFSNNNESTRINELLKVFEELPQANKASITSILDHLIRVHEKETDNKMSLHNLAMVFGPTLLRPGQTQVKQKDPLAASTVDVMAQAGILYCFLQARIKKD
Protein: Lysozyme (EC 3.2.1.17) (CP-1 lysin) (Endolysin) (Muramidase) (P15057)
Organism: Streptococcus phage Cp-1 (Bacteriophage Cp-1)
Function: Responsible for the separation of the host daughter cells at the end of cell division and participates in the liberation of progeny bacteriophage into the medium. Strictly depends on the presence of choline-containing cell walls for activity.
Interaction partners:
Sequence:
MVKKNDLFVDVSSHNGYDITGILEQMGTTNTIIKISESTTYLNPCLSAQVEQSNPIGFYHFARFGGDVAEAEREAQFFLDNVPMQVKYLVLDYEDDPSGDAQANTNACLRFMQMIADAGYKPIYYSYKPFTHDNVDYQQILAQFPNSLWIAGYGLNDGTANFEYFPSMDGIRWWQYSSNPFDKNIVLLDDEEDDKPKTAGTWKQDSKGWWFRRNNGSFPYNKWEKIGGVWYYFDSKGYCLTSEWLKDNEKWYYLKDNGAMATGWVLVGSEWYYMDDSGAMVTGWVKYKNNWYYMTNERGNMVSNEFIKSGKGWYFMNTNGELADNPSFTKEPDGLITVA
Protein: Sodium- and chloride-dependent taurine transporter (Solute carrier family 6 member 6) (P31641)
Organism: Homo sapiens (Human)
Function: Mediates sodium- and chloride-dependent transport of taurine. Mediates transport of beta-alanine. Can also mediate transport of hypotaurine and gamma-aminobutyric acid (GABA) (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:31345061, ECO:0000269|PubMed:31903486}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MATKEKLQCLKDFHKDILKPSPGKSPGTRPEDEAEGKPPQREKWSSKIDFVLSVAGGFVGLGNVWRFPYLCYKNGGGAFLIPYFIFLFGSGLPVFFLEIIIGQYTSEGGITCWEKICPLFSGIGYASVVIVSLLNVYYIVILAWATYYLFQSFQKELPWAHCNHSWNTPHCMEDTMRKNKSVWITISSTNFTSPVIEFWERNVLSLSPGIDHPGSLKWDLALCLLLVWLVCFFCIWKGVRSTGKVVYFTATFPFAMLLVLLVRGLTLPGAGAGIKFYLYPDITRLEDPQVWIDAGTQIFFSYAICLGAMTSLGSYNKYKYNSYRDCMLLGCLNSGTSFVSGFAIFSILGFMAQEQGVDIADVAESGPGLAFIAYPKAVTMMPLPTFWSILFFIMLLLLGLDSQFVEVEGQITSLVDLYPSFLRKGYRREIFIAFVCSISYLLGLTMVTEGGMYVFQLFDYYAASGVCLLWVAFFECFVIAWIYGGDNLYDGIEDMIGYRPGPWMKYSWAVITPVLCVGCFIFSLVKYVPLTYNKTYVYPNWAIGLGWSLALSSMLCVPLVIVIRLCQTEGPFLVRVKYLLTPREPNRWAVEREGATPYNSRTVMNGALVKPTHIIVETMM
Protein: phosphoglycerate mutase (2,3-diphosphoglycerate-dependent) (EC 5.4.2.11) (Q9GU73)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
QEEALAAGKAVKDAGLEFDVAHTSVLTRAQVTLASILKASGHKEIPIQKTWRLNERHYGGLTGLNKAETAAKYGEAQVQIWRRSFDTPPPPMEPGHPYYENIVKDPRYAEGPKPEEFPQFESLKLTIERTLPYWNDVIIPQMKEGKRILIAAHGNSLRGIVKHLDNLSEDAIMALNLPTGIPFVYELDENFKPVVSMQFLGDEETVKKAIEAVAAQGKAK
Protein: Homeobox protein Hox-B5a (Hox-B5) (Homeobox protein Zf-21) (P09014)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.
Subcellular location: Nucleus.
Interaction partners:
- Homeobox protein Hox-B7a
- Homeobox protein Hox-B6a
- Homeobox protein Hox-B6b
- Homeobox protein Hox-B4a
- Homeobox protein Hox-C4a
- Homeobox protein Hox-B3a
Sequence:
MSSYFVNSFSGRYPNGPDYQLLNYGTSSSAMNASYRDSGTMHSGSYGYNYNGMDLSVNRSTSTGHFGAVGDNSRVFQSPAPETRFRQPSSCSLASPEPLPCSNSESLGPKGSSPPSDQSTTTAGNNLNSNTHFTEIDEASASSETEEASHRANNSAPRTQQKQETTATSTTSATSDGQAPQIFPWMRKLHISHDMTGPDGKRARTAYTRYQTLELEKEFHFNRYLTRRRRIEIAHALCLSERQIKIWFQNRRMKWKKDNKLKSMSLATAGSAFQP
Protein: 3'-5' exonuclease Snipper (EC 3.1.15.-) (ERI1 exoribonuclease 2) (Q95RQ4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8IV48}. Nucleus {ECO:0000250|UniProtKB:Q8IV48}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q8IV48}.
Interaction partners:
- Histone RNA hairpin-binding protein
- RRM domain-containing protein
Sequence:
MALIKLARQLGLIDTIYVDGARPDPNNDPEESFNEDEVTEANSVPAKSKKSRKSKRLAMQPYSYVIAVDFEATCWEKQAPPEWREAEIIEFPAVLVNLKTGKIEAEFHQYILPFESPRLSAYCTELTGIQQKTVDSGMPLRTAIVMFNEWLRNEMRARNLTLPKMNKSNILGNCAFVTWTDWDFGICLAKECSRKGIRKPAYFNQWIDVRAIYRSWYKYRPCNFTDALSHVGLAFEGKAHSGIDDAKNLGALMCKMVRDGALFSITKDLTPYQQLNPRFVL
Protein: DNA helicase (EC 3.6.4.12) (Q8TZC3)
Organism: Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
Interaction partners:
- DNA-directed RNA polymerase subunit Rpo3
- Protein implicated in ribosomal biogenesis, Nop56p homolog
- Probable tRNA pseudouridine synthase B
- Transcription initiation factor IIB
- DNA-directed RNA polymerase subunit Rpo5
- Predicted deacetylase
- tRNA
Sequence:
MVEIKEIGEVSTEETSPGAHSHITGLGLDENLKAKPVGDGLVGQEEAREAAGIVVEMVKQGRRAGHGLLLVGPPGTGKTAIAYGIARELGEDVPFVSISGSEIYGTNLSKTEFLQQAIRRAIGVEFTETREVIEGKVESLEIERAKHPLSPYMEVPSGAIIELKTQDDHRRFKVPEEIAIQLVQAGVREGDVIQIDVESGHVTKLGRAKDALEEEEEELLGVHAVELPEGPVQKKKEIKRVVTLHDLDMANVRAGRLLGFREEEITDEIRQKVDERVQKMVDEGEASLVPGVLFIDEAHMLDIEAFAFLNRSLEEEIAPILVMATNRAMAKVRGTDEEAPHGIPGDLLDRMLIARTRPFERHEIHEIIGIRARVQDIQLTDEAHEYLTDLGEEKSIRYATRLLEPARIVAEKEGSEVVEKKHVERVEEVFTDVSDSVEYMERMRRELPVMKYLTG
Protein: aldehyde dehydrogenase (NAD(+)) (EC 1.2.1.3) (A0A1B0GW77)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MWRLPRALCVHAAKTSKLSGPWSRPAAFMSTLLINQPQYAWLKELGLREENEGVYNGSWGGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSCCVVQAGLKLLSSRSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINYSKDLPLAQGIKFQ
Protein: Signal recognition particle subunit SRP54 (EC 3.6.5.4) (Signal recognition particle 54 kDa protein homolog) (P20424)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Signal-recognition-particle (SRP) assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum (ER) membrane. SRP is required for the cotranslational protein translocation for ER import and preferentially recognizes strongly hydrophobic signal sequences. It is involved in targeting the nascent chain-ribosome (RNC) complex to the ER and is proposed to participate in the arrest of nascent chain elongation during membrane targeting. SRP54 binds to the signal sequence of presecretory protein when they emerge from the ribosomes. SRP54 interacts with the scR1 RNA and mediates the association of the resulting SRP-RNC complex with the signal recognition particle receptor (SR) via its alpha subunit SRP101. Both, SRP54 and SRP101, are locked in their GTP bound forms in the SRP-RNC-SR complex, which dissociates upon transferring the signal sequence to the protein-conducting channel (translocon). After signal sequence transfer, SRP54 and SRP101 act as reciprocal GTPase-activating proteins (GAPs), thereby resolving their association.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10676815}. Endoplasmic reticulum {ECO:0000269|PubMed:10676815}.
Interaction partners:
- Signal recognition particle subunit SRP72
- Signal recognition particle subunit SRP21
- Signal recognition particle subunit SEC65
- Signal recognition particle subunit SRP14
- Signal recognition particle subunit SRP68
- Signal recognition particle receptor subunit alpha homolog
- Signal recognition particle receptor subunit beta
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS3
Sequence:
MVLADLGKRINSAVNNAISNTQDDFTTSVDVMLKGIVTALLESDVNIALVSKLRNNIRSQLLSENRSEKSTTNAQTKKLIQKTVFDELCKLVTCEGSEEKAFVPKKRKTNIIMFVGLQGSGKTTSCTKLAVYYSKRGFKVGLVCADTFRAGAFDQLKQNAIRARIPFYGSYTETDPAKVAEEGINKFKKEKFDIIIVDTSGRHHQEEELFQEMIEISNVIKPNQTIMVLDASIGQAAEQQSKAFKESSDFGAIILTKMDGHARGGGAISAVAATNTPIIFIGTGEHIHDLEKFSPKSFISKLLGIGDIESLFEQLQTVSNKEDAKATMENIQKGKFTLLDFKKQMQTIMKMGPLSNIAQMIPGMSNMMNQVGEEETSQKMKKMVYVLDSMTKEELESDGRMFIEEPTRMVRVAKGSGTSVFEVEMILMQQQMMARMAQTATQQQPGAPGANARMPGMPNMPGMPNMPGMPNMPGMPKVTPQMMQQAQQKLKQNPGLMQNMMNMFGGGMGGGMGGGMPDMNEMMKMMQDPQMQQMAKQFGMG
Protein: Vacuolar transporter chaperone complex subunit 1 (Negative regulator of CDC42 protein 1) (Phosphate metabolism protein 4) (SPX-dependent polyphosphate polymerase VTC subunit 1) (Vacuolar membrane polyphosphate polymerase accessory subunit 1) (PolyP polymerase) (P40046)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Accessory subunit of the vacuolar transporter chaperone (VTC) complex. The VTC complex acts as vacuolar polyphosphate polymerase that catalyzes the synthesis of inorganic polyphosphate (polyP) via transfer of phosphate from ATP to a growing polyP chain, releasing ADP. VTC exposes its catalytic domain VTC4 to the cytosol, where the growing polyP chain winds through a tunnel-shaped pocket, integrating cytoplasmic polymer synthesis with polyP membrane translocation. The VTC complex carries 9 vacuolar transmembrane domains, which are likely to constitute the translocation channel into the organelle lumen. PolyP synthesis is tightly coupled to its transport into the vacuole lumen, in order to avoid otherwise toxic intermediates in the cytosol, and it depends on the proton gradient across the membrane, formed by V-ATPase. VTC1 contributes only 3 transmembrane domains to the complex (Probable). The VTC complex also plays a role in vacuolar membrane fusion. Required for SEC18/NSF activity in SNARE priming, membrane binding of LMA1 and V(0) trans-complex formation.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:10480897, ECO:0000269|PubMed:12584253, ECO:0000269|PubMed:19390046}; Multi-pass membrane protein {ECO:0000269|PubMed:10480897}. Cytoplasm, cell cortex {ECO:0000269|PubMed:17079729, ECO:0000269|PubMed:19390046}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:17079729}; Multi-pass membrane protein {ECO:0000269|PubMed:10480897}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:17079729}; Multi-pass membrane protein {ECO:0000269|PubMed:10480897}.
Interaction partners:
- Vacuolar transporter chaperone complex subunit 4
- Vacuolar transporter chaperone 3 complex subunit 3
- Vacuolar transporter chaperone complex subunit 2
- Vacuole transporter chaperone complex subunit 5
- Inorganic phosphate transporter PHO84
- Putative cyclin-dependent kinase inhibitor SPL2
- Phosphate system positive regulatory protein PHO81
- Acid phosphatase PHO12
- Glycerophosphocholine phosphodiesterase GDE1
- Phosphate permease PHO89
Sequence:
MSSAPLLQRTPGKKIALPTRVEPKVFFANERTFLSWLNFTVMLGGLGVGLLNFGDKIGRVSAGLFTFVAMGTMIYALVTYHWRAAAIRRRGSGPYDDRLGPTLLCFFLLVAVIINFILRLKYNDANTKL
Protein: tRNA (cytosine(38)-C(5))-methyltransferase (EC 2.1.1.204) (DNA (cytosine-5)-methyltransferase-like protein 2) (Dnmt2) (DNA methyltransferase homolog HsaIIP) (DNA MTase homolog HsaIIP) (M.HsaIIP) (PuMet) (O14717)
Organism: Homo sapiens (Human)
Function: Specifically methylates cytosine 38 in the anticodon loop of tRNA(Asp).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16424344}.
Interaction partners:
- DNA
- DNA
- DNA
- tRNA
- RNA cytosine C
- 28S rRNA
- tRNA
- Heterogeneous nuclear ribonucleoprotein K
- Putative methyltransferase NSUN7
- 28S rRNA
Sequence:
MEPLRVLELYSGVGGMHHALRESCIPAQVVAAIDVNTVANEVYKYNFPHTQLLAKTIEGITLEEFDRLSFDMILMSPPCQPFTRIGRQGDMTDSRTNSFLHILDILPRLQKLPKYILLENVKGFEVSSTRDLLIQTIENCGFQYQEFLLSPTSLGIPNSRLRYFLIAKLQSEPLPFQAPGQVLMEFPKIESVHPQKYAMDVENKIQEKNVEPNISFDGSIQCSGKDAILFKLETAEEIHRKNQQDSDLSVKMLKDFLEDDTDVNQYLLPPKSLLRYALLLDIVQPTCRRSVCFTKGYGSYIEGTGSVLQTAEDVQVENIYKSLTNLSQEEQITKLLILKLRYFTPKEIANLLGFPPEFGFPEKITVKQRYRLLGNSLNVHVVAKLIKILYE
Protein: DNAation factor DREP-1 (O61464)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
METAANSGDSKKPFKVKDVTRNIKKAVCASSLEEIRSKVAEKFEKCDHLPTIHLDSDGTEIDDEEYFRTLDENTELVAVFPGEHWIDPTHYVTITTPHGNEAGTGNGELNGGGEGDTTDANNSESARIRQLVGQLQNNLCNVSVMNDADLDSLSNMDPNSLVDITGKEFMEQLKDAGRPLCAKRNAEDRLNLLKLKLLKAGAIFCSERYPEDAEAIDREIGRQLNEAESGQMSTTTTSNTRTIEVVQCDNQNTTITITVGEATTTCATASGAMGSSAAEAAANEANANPNRNPNANGDI
Protein: Fibrinogen alpha chain [Cleaved into: Fibrinopeptide A; Fibrinogen alpha chain] (E9PV24)
Organism: Mus musculus (Mouse)
Function: Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the immune response via both innate and T-cell mediated pathways.
Subcellular location: Secreted {ECO:0000269|PubMed:7649481}.
Interaction partners:
- Prothrombin
- Fibrinogen gamma chain
- Fibrinogen beta chain
- Plasminogen
- Albumin
- Integrin beta-3
- Alpha-2-HS-glycoprotein
- Alpha-2-antiplasmin
- Coagulation factor XIII B chain
- Antithrombin-III
Sequence:
MLSLRVTCLILSVASTVWTTDTEDKGEFLSEGGGVRGPRVVERHQSQCKDSDWPFCSDDDWNHKCPSGCRMKGLIDEANQDFTNRINKLKNSLFDFQRNNKDSNSLTRNIMEYLRGDFANANNFDNTYGQVSEDLRRRIEILRRKVIEKAQQIQALQSNVRAQLIDMKRLEVDIDIKIRSCKGSCSRAVNREINLQDYEGHQKQLQQVIAKELLPTKDRQYLPALKMSPVPDLVPGSFKSQLQEAPPEWKALTEMRQMRMELERPGKDGGSRGDSPGDSRGDSRGDFATRGPGSKAENPTNPGPGGSGYWRPGNSGSGSDGNRNPGTTGSDGTGDWGTGSPRPGSDSGNFRPANPNWGVFSEFGDSSSPATRKEYHTGKAVTSKGDKELLIGKEKVTSSGTSTTHRSCSKTITKTVTGPDGRREVVKEVITSDDGSDCGDATELDISHSFSGSLDELSERHPDLSGFFDNHFGLISPNFKEFGSKTHSDSDILTNIEDPSSHVPEFSSSSKTSTVKKQVTKTYKMADEAGSEAHREGETRNTKRGRARARPTRDCDDVLQTQTSGAQNGIFSIKPPGSSKVFSVYCDQETSLGGWLLIQQRMDGSLNFNRTWQDYKRGFGSLNDKGEGEFWLGNDYLHLLTLRGSVLRVELEDWAGKEAYAEYHFRVGSEAEGYALQVSSYRGTAGDALVQGSVEEGTEYTSHSNMQFSTFDRDADQWEENCAEVYGGGWWYNSCQAANLNGIYYPGGTYDPRNNSPYEIENGVVWVPFRGADYSLRAVRMKIRPLVGQ
Protein: Profilin (E7F0A1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Actin alpha 1, skeletal muscle b.
- Actin, cytoplasmic 2
- Actin, cytoplasmic 1
- Vasodilator-stimulated phosphoprotein
- FH2 domain-containing protein.
- Diaphanous-related formin 2.
- Profilin
- Profilin
- Profilin
- Transitional endoplasmic reticulum ATPase
Sequence:
MSWDSYISSLTQSEWVDDAVILGATPGQESIWASAPGGWLSGVTAAEVKAILNTDRGKLFCNGVTLAGKRCTVVRDALFVDGQFTMDVKMKTSEKEPDPFSLTIGKSISALIIAKGVKDAHGGKVNPPVFDMALYLRKMNM
Protein: Gartenzwerg, isoform A (A1Z8W9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MALPGNGIYVVRGEMATLMTAMRRGTRWNATAYVDDENDSLLKLFIDLKHELNRIEDLRQIEPQVFLAPFLEVIRTADATGPLTSLALASVNKLLSYGLIDPTSPNLADIVERIADAVTHARFMGTDQSSDGVTFMRVIEVLHTLIRSPEGAAVSNVSMCEVMLSCFKISFEPRLSELLRRSAEKSLKDMVLLFFMRLPQFAEERSDTMLQKRFTIGDAASGATQEKLKRKTVAQAQTAPRKSSAVEEPPQTPQSANLTVPGHLKAPILATTPASPAGNILDMQGKITQTPTTTASTGEDETTVPETPVIQVESTESEPLLDGETGEATSTLAEANSSEYINSVGVRFTQQSTDHDVTSLSPYGLPFIQELFRFLIILCNPLDKQNSDSMMHTGLSLLTVAFEVAADNIGKYEGLLELVKDDLCRNLISLLSSERLSIFAADLQLCFLLFESLRGHLKFQLEAYLRKLSEIIASDNPKTPYEMRELALDNLLQLWRIPGFVTELYINYDCDLYCTDMFESLTNLLSKYTLSATNAVYSTHIISMDTLLSVIDSIERNCAASKNSSNNRESLPEAAPATGGSRHSRHNSGLEGIVIDSGNSVAAEEKVENIASFINASSHRLRLQSGGEGVGITSEQLAKVKQKKRLLSQGTERFNQRPEKGIQYLQEHGILNAELDPMQVALFLRENPGLDKKMIGEYISKKKNVDSKILINFVDSFDFTGLRVDQALRLYLETFRLPGEAPLIFLVLEHFSDHWHKQNQDPFANVDAAFRLAYAIIMLNMDQHNSNAKRLNVPMTLEDFTKNLRGLNGGEDFDQEMLAQVFNAIKNEEIVMPAEQTGLVRENYQWKVLLRRGDTHDGHFHYVHDASYDVEIFNIVWGASLSALSFMFDKSTETGYQRTLAGFSKSAAISAHYNLHSDFDALVLTLCKFTTLLSSVEQHEPAPANNETQQAVNFGLNGKAQAAMRTVFLLVHDYGDCLRESWKHILDLYLQLFRLKLLPKSLIEVEDFCEANGKAMLILEKPREKQESGLFSSLYSFISSEGQREPTYEEQDFIKLGRKCIKECQLDQMLQESKFVQLESLQELLKCVLALLKAPQGHKSIGLPYAEDQTVFWMEFLVKIVVHNRDRMIPLWPAVRDQMYLLLMGSASCGYDYLLNRCIVAVLKLAIYLMRNEELCPIVLQSLKMLLMLKPALLLRISKQISIGIYELLKTSAQNIHSEQDWQIIFNLLECVGAGAVPPNYDDAQLPLPPNGSAKSDGAISGEEDATAVPERGYTSDSEITKASAAPAVSSPSAENWILVNNKDSELTTASRPQSPPSLSAPPVNTLVYNCQLLDHAPFALFKCWDSLAFIVRSVAHITPYNFEACVRCIRIFVEACRDGGIRQRRKLESAAKQKSSKKRSERKPGMASSASSSNLTLLTGDPSDNQINGNAAEQEDLAQRYEQLSIQLLDLMYTLYTRTAQIFRWWAEEGCTVPQSAALWSPGWCPLLQGIARLAMDRRREVRTHAISCLQQRALLVHDLQTLSGTEWCSCFHQVLFPLLNELLPESNAAGQLDAALLEESRIRTATIMSKVFLQHLTTLIELGNAFNELWLDILDYIERFMKVGSDTLSEQMQEILKNMLLVMHSVRVFHNQDGSLQQALWELTWRRIGEFLPNLKEELFHDEDSITPAVSLDYTQIRFAHSTGTTDYSLSLPLYGYSPKISSISASKCDTLPATQRKKPWAKLRSKLKLLKKVGKKN
Protein: Glucose-6-phosphate isomerase (GPI) (EC 5.3.1.9) (Phosphoglucose isomerase) (PGI) (Phosphohexose isomerase) (PHI) (P9WN69)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00473}.
Interaction partners:
- Triosephosphate isomerase
- ATP-dependent 6-phosphofructokinase
- Enolase
- Pyruvate kinase
- Transaldolase
- Probable phosphoglucomutase PgmA
- Transketolase
- Glyceraldehyde-3-phosphate dehydrogenase
- Fructose-bisphosphate aldolase
- Glucose-6-phosphate 1-dehydrogenase 2
Sequence:
MTSAPIPDITATPAWDALRRHHDQIGNTHLRQFFADDPGRGRELTVSVGDLYIDYSKHRVTRETLALLIDLARTAHLEERRDQMFAGVHINTSEDRAVLHTALRLPRDAELVVDGQDVVTDVHAVLDAMGAFTDRLRSGEWTGATGKRISTVVNIGIGGSDLGPVMVYQALRHYADAGISARFVSNVDPADLIATLADLDPATTLFIVASKTFSTLETLTNATAARRWLTDALGDAAVSRHFVAVSTNKRLVDDFGINTDNMFGFWDWVGGRYSVDSAIGLSLMTVIGRDAFADFLAGFHIIDRHFATAPLESNAPVLLGLIGLWYSNFFGAQSRTVLPYSNDLSRFPAYLQQLTMESNGKSTRADGSPVSADTGEIFWGEPGTNGQHAFYQLLHQGTRLVPADFIGFAQPLDDLPTAEGTGSMHDLLMSNFFAQTQVLAFGKTAEEIAADGTPAHVVAHKVMPGNRPSTSILASRLTPSVLGQLIALYEHQVFTEGVVWGIDSFDQWGVELGKTQAKALLPVITGAGSPPPQSDSSTDGLVRRYRTERGRAG
Protein: Protein AUXIN SIGNALING F-BOX 3 (Q9LPW7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Confers sensitivity to the virulent bacterial pathogen P.syringae (By similarity). Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Auxin receptor that mediates Aux/IAA proteins proteasomal degradation and auxin-regulated transcription. Involved in embryogenesis regulation by auxin.
Subcellular location: Nucleus {ECO:0000269|PubMed:15992545}.
Interaction partners:
- Auxin transporter protein 1
- Auxin response factor 6
- Protein NRT1/ PTR FAMILY 6.3
- Protein NLP7
- Dof zinc finger protein DOF5.4
- Auxin response factor 8
- MADS-box transcription factor ANR1
- Auxin response factor 19
- Auxin response factor 7
- Cullin-1
Sequence:
MNYFPDEVIEHVFDFVASHKDRNSISLVCKSWHKIERFSRKEVFIGNCYAINPERLIRRFPCLKSLTLKGKPHFADFNLVPHEWGGFVHPWIEALARSRVGLEELRLKRMVVTDESLDLLSRSFANFKSLVLVSCEGFTTDGLASIAANCRHLRELDLQENEIDDHRGQWLNCFPDSCTTLMSLNFACLKGETNVAALERLVARSPNLKSLKLNRAVPLDALARLMSCAPQLVDLGVGSYENEPDPESFAKLMTAIKKYTSLRSLSGFLEVAPLCLPAFYPICQNLISLNLSYAAEIQGNHLIKLIQLCKRLQRLWILDSIGDKGLAVVAATCKELQELRVFPSDVHGEEDNNASVTEVGLVAISAGCPKLHSILYFCKQMTNAALIAVAKNCPNFIRFRLCILEPHKPDHITFQSLDEGFGAIVQACKGLRRLSVSGLLTDQVFLYIGMYAEQLEMLSIAFAGDTDKGMLYVLNGCKKMRKLEIRDSPFGNAALLADVGRYETMRSLWMSSCEVTLGGCKRLAQNSPRLNVEIINENENNGMEQNEEDEREKVDKLYLYRTVVGTRKDAPPYVRIL
Protein: Hattifattener, isoform C (Hattifattener, isoform E) (Q9VQ25)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRPGRTTTALPAATTPLLLLLPLILGRLHVAHAQCPWQRDVPDLQTSCICAYNLGRELSVQCDQVDFSQLLAAMNTHARLKPVDLLYVNNSTISELPDAVFSNLSLHNLQLSSCGIQRIATGAFKGQESVLRNLNLQDNLLADVPVEALKVLGKLNLLDLSKNQLSHIPDDAFVGLTKLSTLKLNDNNVTLASNAFRGLEQSLKNLNLKGTKQRKVPESIRGLKSLAFLDLSQNGIKELPGAGGIRVFDGLDALTALNLERNLIQSIGETAFAGVRKTLSSLSLLNNLLAEFPIGAVHSLKELRVLDIGFNLLTSLPEAAFRGNPGITLLALDGNPLSSVPEGAFAHLNATLRGLSLGGRFLHCDCKLRWVAEWIRNGDLQVTSRERNPQFCGTPPRFRDRGFYSIQPEELSCPDIADAALRGPVGLADNLKPTLPSSPDSVEYETGTGTGTVGTGTAASAPVTSSVSSSTSTTTPTTTTTTTTAEPTTRRSTTRPPTKSTTTISATTASPASNPPVNGTGTVQATSITTSSSSSSSSSTSTGHGNGKQAPGWRQGVTNGNGNSGVGGAGGLHKPQRPPLVLGYPPQRGTRIDDANEVQVKHAFRQDSSVIIQWDSDTANILGFRVVYRLFGEKAFKQGPPLESSEREFKIKNVPAQECIIVCVISLEELHVTPETVPYQQCREVRTVASQASNMDKITIAASAAICGTIIVAVIVFIAASRRSRKLQSSQQKSPLPIGGLPVNCCGPTGSPGPLGSIATLSAFNNHKEWDQVSAYSGRSIPRPRIYPVEQPDDMRSHFSGMPGKVGKSSRSLADGQSQHSFSNNSHRGYLGSAFPSNLVNSRPELRQSRQSLAAASERMSRASYAGSIHGGNGGGGGLGGNGGGGGNGLPVSSLMAMSGMVGGGGPASIASSARRSRPRSRSREQLNTTHIHNHRPGSRYSQAGSTHTLNNYCDTSDNWTDHDMDIYMARNPTTRNGLVPL
Protein: 5-formyltetrahydrofolate cyclo-ligase-like protein COG0212 (Protein CLUSTERS OF ORTHOLOGOUS GROUP 212) (Q9SRE0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in thiamine metabolism. Does not possess 5-formyltetrahydrofolate cyclo-ligase activity in vitro.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:21538139}.
Interaction partners:
- 5-formyltetrahydrofolate cyclo-ligase, mitochondrial
- Bifunctional protein FolD 1
- Bifunctional protein FolD 2
- Bifunctional protein FolD 4, chloroplastic
- Bifunctional protein FolD 3, chloroplastic
- Formate--tetrahydrofolate ligase
- Phosphoribosylglycinamide formyltransferase, chloroplastic
- Hydroxyethylthiazole kinase
- Nudix hydrolase 24, chloroplastic
- Serine hydroxymethyltransferase 1, mitochondrial
Sequence:
MIRLSPGFAINPRFRSDSFVNSQKPPFLSVQIGSQRRNLSRIGSENGDGVAFDAVAYEADRLSLDAAAMEDMAETAKKELESDPDSDPKAWKWVIRKKMWDLMEARNYAMSPRPVHHRIPNFVGASAAARKLAELDAFRMAMVVKVNPDSPQKQIRFLTLSGEKKLLTPQPRLRTGFFSVLESDLLKPETIMEACTSVGVAKYGRAIGLDEKIKVDLIVIGSVAVNPQTGARLGKGEGFAELEYGMLRYMGAIDDSTPVVTTVHDCQLVDDIPLEKLAIHDVPVDIICTPTRVIFTNTPIPKPQGIYWDKLSPEKLRQIRILRELKNRLEKKTGRKLPTGPSEKLPPTAERKRR